CFBA_METMA
ID CFBA_METMA Reviewed; 130 AA.
AC Q8PZH6;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Sirohydrochlorin cobaltochelatase {ECO:0000255|HAMAP-Rule:MF_00785};
DE EC=4.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00785};
DE AltName: Full=CbiXS {ECO:0000255|HAMAP-Rule:MF_00785};
DE AltName: Full=Sirohydrochlorin nickelchelatase {ECO:0000255|HAMAP-Rule:MF_00785};
DE EC=4.99.1.11 {ECO:0000255|HAMAP-Rule:MF_00785};
GN Name=cbiX {ECO:0000255|HAMAP-Rule:MF_00785};
GN Synonyms=cfbA {ECO:0000255|HAMAP-Rule:MF_00785}; OrderedLocusNames=MM_0517;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC -!- FUNCTION: Catalyzes the insertion of Co(2+) into sirohydrochlorin as
CC part of the anaerobic pathway to cobalamin biosynthesis. Involved in
CC the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme
CC F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which
CC plays a key role in methanogenesis and anaerobic methane oxidation.
CC Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni-
CC sirohydrochlorin. {ECO:0000255|HAMAP-Rule:MF_00785}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin;
CC Xref=Rhea:RHEA:15893, ChEBI:CHEBI:15378, ChEBI:CHEBI:48828,
CC ChEBI:CHEBI:58351, ChEBI:CHEBI:60049; EC=4.99.1.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00785};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + Ni-sirohydrochlorin = Ni(2+) + sirohydrochlorin;
CC Xref=Rhea:RHEA:52796, ChEBI:CHEBI:15378, ChEBI:CHEBI:49786,
CC ChEBI:CHEBI:58351, ChEBI:CHEBI:136841; EC=4.99.1.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00785};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC step 1/10. {ECO:0000255|HAMAP-Rule:MF_00785}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00785}.
CC -!- SIMILARITY: Belongs to the CbiX family. CbiXS subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00785}.
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DR EMBL; AE008384; AAM30213.1; -; Genomic_DNA.
DR RefSeq; WP_011032469.1; NC_003901.1.
DR AlphaFoldDB; Q8PZH6; -.
DR SMR; Q8PZH6; -.
DR STRING; 192952.MM_0517; -.
DR EnsemblBacteria; AAM30213; AAM30213; MM_0517.
DR GeneID; 24876802; -.
DR KEGG; mma:MM_0517; -.
DR PATRIC; fig|192952.21.peg.617; -.
DR eggNOG; arCOG02246; Archaea.
DR HOGENOM; CLU_065901_2_1_2; -.
DR OMA; HEHEKLE; -.
DR UniPathway; UPA00148; UER00223.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016852; F:sirohydrochlorin cobaltochelatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019251; P:anaerobic cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR HAMAP; MF_00785; CbiX; 1.
DR InterPro; IPR002762; CbiX-like.
DR InterPro; IPR023652; SiroHydchlorin_Cochelatase.
DR Pfam; PF01903; CbiX; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Cobalt; Lyase; Metal-binding; Methanogenesis;
KW Nickel; Reference proteome.
FT CHAIN 1..130
FT /note="Sirohydrochlorin cobaltochelatase"
FT /id="PRO_0000150358"
FT ACT_SITE 12
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 12
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 12
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 73..78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 78
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 78
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
SQ SEQUENCE 130 AA; 13980 MW; 46C5232FE045B3E3 CRC64;
MTEKLGILAI GHGSKLPYNK EVVTQIANYI AQKHSDVVVR AGFMENSEPT LEEAIEGFSG
TGVTKISAVP VFLASGVHIT KDIPEILSLD KEGCGILEID GKEVPLCYAK PLGADELIAE
LVFKRVQESL
