4C1N | pdb_00004c1n

Corrinoid protein reactivation complex with activator

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	AcsC C-terminal domain-like	8089866	3002396	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Dihydropteroate synthetase-like	8089865	3000643	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	AcsC Fe-S domain-like	8089863	3002395	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Dihydropteroate synthetase-like	8089865	3000643	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	AcsC Fe-S domain-like	8089863	3002395	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	AcsC C-terminal domain-like	8089866	3002396	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	AcsC Fe-S domain-like	8089863	3002395	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Dihydropteroate synthetase-like	8089865	3000643	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	AcsC C-terminal domain-like	8089866	3002396	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Dihydropteroate synthetase-like	8089865	3000643	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	AcsC Fe-S domain-like	8089863	3002395	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	AcsC C-terminal domain-like	8089866	3002396	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Dihydropteroate synthetase-like	8089867	3000643	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Dihydropteroate synthetase-like	8089867	3000643	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Dihydropteroate synthetase-like	8089867	3000643	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Dihydropteroate synthetase-like	8089867	3000643	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	CdhD_N	e4c1nA3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: CdhD_N	ECOD (1.6)
A	CdhD_C	e4c1nA1	A: a/b three-layered sandwiches	X: B12 binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	H: B12 binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	T: B12 binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit	F: CdhD_C	ECOD (1.6)
A	FeS	e4c1nA2	A: few secondary structure elements	X: Fe-S cluster binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	H: Fe-S cluster binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	T: Fe-S cluster binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit	F: FeS	ECOD (1.6)
C	CdhD_N	e4c1nC3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: CdhD_N	ECOD (1.6)
C	CdhD_C	e4c1nC1	A: a/b three-layered sandwiches	X: B12 binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	H: B12 binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	T: B12 binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit	F: CdhD_C	ECOD (1.6)
C	FeS	e4c1nC2	A: few secondary structure elements	X: Fe-S cluster binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	H: Fe-S cluster binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	T: Fe-S cluster binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit	F: FeS	ECOD (1.6)
E	CdhD_N	e4c1nE3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: CdhD_N	ECOD (1.6)
E	CdhD_C	e4c1nE1	A: a/b three-layered sandwiches	X: B12 binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	H: B12 binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	T: B12 binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit	F: CdhD_C	ECOD (1.6)
E	FeS	e4c1nE2	A: few secondary structure elements	X: Fe-S cluster binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	H: Fe-S cluster binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	T: Fe-S cluster binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit	F: FeS	ECOD (1.6)
G	CdhD_N	e4c1nG3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: CdhD_N	ECOD (1.6)
G	CdhD_C	e4c1nG1	A: a/b three-layered sandwiches	X: B12 binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	H: B12 binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	T: B12 binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit	F: CdhD_C	ECOD (1.6)
G	FeS	e4c1nG2	A: few secondary structure elements	X: Fe-S cluster binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	H: Fe-S cluster binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit (From Topology)	T: Fe-S cluster binding domain in carbon monoxide dehydrogenase corrinoid/iron-sulfur protein gamma subunit	F: FeS	ECOD (1.6)
B	CdhD_N	e4c1nB1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: CdhD_N	ECOD (1.6)
D	CdhD_N	e4c1nD1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: CdhD_N	ECOD (1.6)
F	CdhD_N	e4c1nF1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: CdhD_N	ECOD (1.6)
H	CdhD_N	e4c1nH1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: CdhD_N	ECOD (1.6)
I	EUF08308	e4c1nI3	A: a+b two layers	X: Ribosomal protein L31e-like	H: Reductive activator for corrinoid/iron-sulfur protein second domain (From Topology)	T: Reductive activator for corrinoid/iron-sulfur protein second domain	F: EUF08308	ECOD (1.6)
I	DUF4445_C	e4c1nI1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: DUF4445_C	ECOD (1.6)
I	DUF4445_N	e4c1nI2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: DUF4445_N	ECOD (1.6)
J	EUF08308	e4c1nJ3	A: a+b two layers	X: Ribosomal protein L31e-like	H: Reductive activator for corrinoid/iron-sulfur protein second domain (From Topology)	T: Reductive activator for corrinoid/iron-sulfur protein second domain	F: EUF08308	ECOD (1.6)
J	DUF4445_C	e4c1nJ1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: DUF4445_C	ECOD (1.6)
J	DUF4445_N	e4c1nJ2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: DUF4445_N	ECOD (1.6)
L [auth X]	EUF08308	e4c1nX3	A: a+b two layers	X: Ribosomal protein L31e-like	H: Reductive activator for corrinoid/iron-sulfur protein second domain (From Topology)	T: Reductive activator for corrinoid/iron-sulfur protein second domain	F: EUF08308	ECOD (1.6)
L [auth X]	DUF4445_C	e4c1nX1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: DUF4445_C	ECOD (1.6)
L [auth X]	DUF4445_N	e4c1nX2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: DUF4445_N	ECOD (1.6)
K	EUF08308	e4c1nK3	A: a+b two layers	X: Ribosomal protein L31e-like	H: Reductive activator for corrinoid/iron-sulfur protein second domain (From Topology)	T: Reductive activator for corrinoid/iron-sulfur protein second domain	F: EUF08308	ECOD (1.6)
K	DUF4445_C	e4c1nK1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: DUF4445_C	ECOD (1.6)
K	DUF4445_N	e4c1nK2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: DUF4445_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.15.40	Mainly Alpha	Orthogonal Bundle	3-methyladenine DNA Glycosylase II	Chain A, domain 3	CATH (4.3.0)
A	3.20.20.20	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Dihydropteroate synthase-like	CATH (4.3.0)
A	3.40.50.11600	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
C	1.10.15.40	Mainly Alpha	Orthogonal Bundle	3-methyladenine DNA Glycosylase II	Chain A, domain 3	CATH (4.3.0)
C	3.20.20.20	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Dihydropteroate synthase-like	CATH (4.3.0)
C	3.40.50.11600	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
E	1.10.15.40	Mainly Alpha	Orthogonal Bundle	3-methyladenine DNA Glycosylase II	Chain A, domain 3	CATH (4.3.0)
E	3.20.20.20	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Dihydropteroate synthase-like	CATH (4.3.0)
E	3.40.50.11600	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
G	1.10.15.40	Mainly Alpha	Orthogonal Bundle	3-methyladenine DNA Glycosylase II	Chain A, domain 3	CATH (4.3.0)
G	3.20.20.20	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Dihydropteroate synthase-like	CATH (4.3.0)
G	3.40.50.11600	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	3.20.20.20	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Dihydropteroate synthase-like	CATH (4.3.0)
D	3.20.20.20	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Dihydropteroate synthase-like	CATH (4.3.0)
F	3.20.20.20	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Dihydropteroate synthase-like	CATH (4.3.0)
H	3.20.20.20	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Dihydropteroate synthase-like	CATH (4.3.0)
I	3.10.20.880	Alpha Beta	Roll	Ubiquitin-like (UB roll)		CATH (4.3.0)
I	3.30.420.480	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)
J	3.10.20.880	Alpha Beta	Roll	Ubiquitin-like (UB roll)		CATH (4.3.0)
J	3.30.420.480	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)
L [auth X]	3.10.20.880	Alpha Beta	Roll	Ubiquitin-like (UB roll)		CATH (4.3.0)
L [auth X]	3.30.420.480	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)
K	3.10.20.880	Alpha Beta	Roll	Ubiquitin-like (UB roll)		CATH (4.3.0)
K	3.30.420.480	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C, E, G	PF04060	Putative Fe-S cluster (FeS)	Putative Fe-S cluster	This family includes a domain with four conserved cysteines that probably form an Fe-S redox cluster.	Domain
A, C, E, G	PF03599	CO dehydrogenase/acetyl-CoA synthase delta subunit (CdhD)	CO dehydrogenase/acetyl-CoA synthase delta subunit	-	Family
B, D, F, H	PF03599	CO dehydrogenase/acetyl-CoA synthase delta subunit (CdhD)	CO dehydrogenase/acetyl-CoA synthase delta subunit	-	Family
I, J, L [auth X]	PF17651	RACo middle region (Raco_middle)	RACo middle region	This family includes reductive activator of CoFeSP (RACo) proteins, Swiss:Q3ACS2. Structure analysis of RACo indicate that it contains 4 regions: N-terminal region Pfam:PF00111 (residues 3-94) binding the [2Fe-2S] cluster, a linker region (residues 9 ...	This family includes reductive activator of CoFeSP (RACo) proteins, Swiss:Q3ACS2. Structure analysis of RACo indicate that it contains 4 regions: N-terminal region Pfam:PF00111 (residues 3-94) binding the [2Fe-2S] cluster, a linker region (residues 95-125), the middle region (residues 126-206), and the large C-terminal domain Pfam:PF14574 (residues 207-630). This entry pertains to the middle region. This region contains residues in their alpha-helices (H6 and H7) that mediate dimerization with subdomain I of the C-terminal domain.	Domain
I, J, L [auth X]	PF17650	RACo linker region (RACo_linker)	RACo linker region	This family includes reductive activator of CoFeSP (RACo) proteins, Swiss:Q3ACS2. Structure analysis of RACo indicate that it contains 4 regions: N-terminal region Pfam:PF00111 (residues 3-94) binding the [2Fe-2S] cluster, a linker region (residues 9 ...	This family includes reductive activator of CoFeSP (RACo) proteins, Swiss:Q3ACS2. Structure analysis of RACo indicate that it contains 4 regions: N-terminal region Pfam:PF00111 (residues 3-94) binding the [2Fe-2S] cluster, a linker region (residues 95-125), the middle region (residues 126-206), and the large C-terminal domain Pfam:PF14574 (residues 207-630). This entry pertains to the linker region. The linker region is only present in RACE (reductive activases for corrinoid enzymes) protein sequences with the N-terminal [2Fe-2S] cluster family Pfam:PF00111 and is absent in the RamA-like RACE proteins, suggesting that the linker domain and the N-terminal domain form one functional unit [1].	Domain
I, J, L [auth X]	PF14574	C-terminal domain of RACo the ASKHA domain (RACo_C_ter)	C-terminal domain of RACo the ASKHA domain	This family includes reductive activator of CoFeSP (RACo) proteins, Swiss:Q3ACS2. Structure analysis of RACo indicate that it contains 4 regions: N-terminal region Pfam:PF00111 (residues 3-94) binding the [2Fe-2S] cluster, a linker region (residues 9 ...	This family includes reductive activator of CoFeSP (RACo) proteins, Swiss:Q3ACS2. Structure analysis of RACo indicate that it contains 4 regions: N-terminal region Pfam:PF00111 (residues 3-94) binding the [2Fe-2S] cluster, a linker region (residues 95-125), the middle region (residues 126-206), and the large C-terminal domain (residues 207-630). This entry is specific for the C-terminal domain which harbors the ATP-binding site. Structural studies show that the C-terminal domain contains the conserved beta-beta-beta-alpha-beta-alpha-beta-alpha topology characteristic of the ASKHA (acetate and sugar kinases/heat shock protein 70/actin). Despite the low-sequence identity shared between members of the ASKHA super family, they show a common central fold. Members of the ASKHA include proteins that catalyze phosphoryl transfers or hydrolysis of ATP in a variety of biological contexts. Asp, Asn, Glu, and Gln residues are well conserved in the core of the ASKHA proteins, where they interact with the phosphates of ATP and the bound Mg2+ ions.	Domain
K	PF17651	RACo middle region (Raco_middle)	RACo middle region	This family includes reductive activator of CoFeSP (RACo) proteins, Swiss:Q3ACS2. Structure analysis of RACo indicate that it contains 4 regions: N-terminal region Pfam:PF00111 (residues 3-94) binding the [2Fe-2S] cluster, a linker region (residues 9 ...	This family includes reductive activator of CoFeSP (RACo) proteins, Swiss:Q3ACS2. Structure analysis of RACo indicate that it contains 4 regions: N-terminal region Pfam:PF00111 (residues 3-94) binding the [2Fe-2S] cluster, a linker region (residues 95-125), the middle region (residues 126-206), and the large C-terminal domain Pfam:PF14574 (residues 207-630). This entry pertains to the middle region. This region contains residues in their alpha-helices (H6 and H7) that mediate dimerization with subdomain I of the C-terminal domain.	Domain
K	PF17650	RACo linker region (RACo_linker)	RACo linker region	This family includes reductive activator of CoFeSP (RACo) proteins, Swiss:Q3ACS2. Structure analysis of RACo indicate that it contains 4 regions: N-terminal region Pfam:PF00111 (residues 3-94) binding the [2Fe-2S] cluster, a linker region (residues 9 ...	This family includes reductive activator of CoFeSP (RACo) proteins, Swiss:Q3ACS2. Structure analysis of RACo indicate that it contains 4 regions: N-terminal region Pfam:PF00111 (residues 3-94) binding the [2Fe-2S] cluster, a linker region (residues 95-125), the middle region (residues 126-206), and the large C-terminal domain Pfam:PF14574 (residues 207-630). This entry pertains to the linker region. The linker region is only present in RACE (reductive activases for corrinoid enzymes) protein sequences with the N-terminal [2Fe-2S] cluster family Pfam:PF00111 and is absent in the RamA-like RACE proteins, suggesting that the linker domain and the N-terminal domain form one functional unit [1].	Domain
K	PF14574	C-terminal domain of RACo the ASKHA domain (RACo_C_ter)	C-terminal domain of RACo the ASKHA domain	This family includes reductive activator of CoFeSP (RACo) proteins, Swiss:Q3ACS2. Structure analysis of RACo indicate that it contains 4 regions: N-terminal region Pfam:PF00111 (residues 3-94) binding the [2Fe-2S] cluster, a linker region (residues 9 ...	This family includes reductive activator of CoFeSP (RACo) proteins, Swiss:Q3ACS2. Structure analysis of RACo indicate that it contains 4 regions: N-terminal region Pfam:PF00111 (residues 3-94) binding the [2Fe-2S] cluster, a linker region (residues 95-125), the middle region (residues 126-206), and the large C-terminal domain (residues 207-630). This entry is specific for the C-terminal domain which harbors the ATP-binding site. Structural studies show that the C-terminal domain contains the conserved beta-beta-beta-alpha-beta-alpha-beta-alpha topology characteristic of the ASKHA (acetate and sugar kinases/heat shock protein 70/actin). Despite the low-sequence identity shared between members of the ASKHA super family, they show a common central fold. Members of the ASKHA include proteins that catalyze phosphoryl transfers or hydrolysis of ATP in a variety of biological contexts. Asp, Asn, Glu, and Gln residues are well conserved in the core of the ASKHA proteins, where they interact with the phosphates of ATP and the bound Mg2+ ions.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C, E, G	CARBON MONOXIDE DEHYDROGENASE CORRINOID/IRON-SULFUR PROTEIN, GAMMA SUBUNIT	transferase activity, transferring one-carbon groups transferase activity methyltransferase activity catalytic activity iron-sulfur cluster binding binding 4 iron, 4 sulfur cluster binding metal cluster binding small molecule binding cation binding transition metal ion binding iron ion binding ion binding metal ion binding	catabolic process organophosphate catabolic process nucleoside phosphate catabolic process acetyl-CoA metabolic process nucleobase-containing compound metabolic process acyl-CoA metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process small molecule metabolic process sulfur compound metabolic process amide metabolic process thioester metabolic process phosphorus metabolic process acetyl-CoA catabolic process catabolic process organophosphate catabolic process nucleoside phosphate catabolic process acetyl-CoA metabolic process nucleobase-containing compound metabolic process acyl-CoA metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process small molecule metabolic process sulfur compound metabolic process amide metabolic process thioester metabolic process phosphorus metabolic process acetyl-CoA catabolic process nucleoside phosphate metabolic process primary metabolic process purine-containing compound catabolic process nucleobase-containing compound catabolic process purine-containing compound metabolic process sulfur compound catabolic process organophosphate metabolic process metabolic process cellular process	-
B, D, F, H	CO DEHYDROGENASE/ACETYL-COA SYNTHASE, IRON-SULFUR PROTEIN	-	-	-
I, J, L [auth X]	IRON-SULFUR CLUSTER BINDING PROTEIN	iron-sulfur cluster binding 2 iron, 2 sulfur cluster binding binding metal cluster binding small molecule binding cation binding ion binding metal ion binding	-	-
K	IRON-SULFUR CLUSTER BINDING PROTEIN	iron-sulfur cluster binding 2 iron, 2 sulfur cluster binding binding metal cluster binding small molecule binding cation binding ion binding metal ion binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C, E, G	IPR016218	Acetyl-CoA decarbonylase/synthase complex, gamma subunit	Family
A, C, E, G	IPR016041	CO dehydrogenase/acetyl-CoA synthase delta subunit, TIM barrel	Domain
A, C, E, G	IPR007202	4Fe-4S domain	Domain
A, C, E, G	IPR011005	Dihydropteroate synthase-like superfamily	Homologous Superfamily
A, C, E, G	IPR051069	Acetyl-CoA decarbonylase/synthase complex subunit	Family
B, D, F, H	IPR016041	CO dehydrogenase/acetyl-CoA synthase delta subunit, TIM barrel	Domain
B, D, F, H	IPR011005	Dihydropteroate synthase-like superfamily	Homologous Superfamily
B, D, F, H	IPR051069	Acetyl-CoA decarbonylase/synthase complex subunit	Family
I, J, L [auth X]	IPR041414	RACo-like, middle region	Domain
I, J, L [auth X]	IPR036010	2Fe-2S ferredoxin-like superfamily	Homologous Superfamily
I, J, L [auth X]	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain	Domain
I, J, L [auth X]	IPR043129	ATPase, nucleotide binding domain	Homologous Superfamily
I, J, L [auth X]	IPR012675	Beta-grasp domain superfamily	Homologous Superfamily
I, J, L [auth X]	IPR042259	RACo-like, middle domain superfamily	Homologous Superfamily
I, J, L [auth X]	IPR027980	RACo, C-terminal	Domain
I, J, L [auth X]	IPR040506	RACo linker region	Domain
I, J, L [auth X]	IPR052911	Corrinoid activation enzyme	Family
K	IPR041414	RACo-like, middle region	Domain
K	IPR036010	2Fe-2S ferredoxin-like superfamily	Homologous Superfamily
K	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain	Domain
K	IPR043129	ATPase, nucleotide binding domain	Homologous Superfamily
K	IPR012675	Beta-grasp domain superfamily	Homologous Superfamily
K	IPR042259	RACo-like, middle domain superfamily	Homologous Superfamily
K	IPR027980	RACo, C-terminal	Domain
K	IPR040506	RACo linker region	Domain
K	IPR052911	Corrinoid activation enzyme	Family