CFBA_METBU
ID CFBA_METBU Reviewed; 131 AA.
AC Q12X56;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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};
GN OrderedLocusNames=Mbur_1035;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
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; CP000300; ABE51970.1; -; Genomic_DNA.
DR RefSeq; WP_011499119.1; NC_007955.1.
DR AlphaFoldDB; Q12X56; -.
DR SMR; Q12X56; -.
DR STRING; 259564.Mbur_1035; -.
DR EnsemblBacteria; ABE51970; ABE51970; Mbur_1035.
DR GeneID; 3998775; -.
DR KEGG; mbu:Mbur_1035; -.
DR HOGENOM; CLU_065901_2_1_2; -.
DR OMA; ERAMEVM; -.
DR OrthoDB; 93992at2157; -.
DR UniPathway; UPA00148; UER00223.
DR Proteomes; UP000001979; 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..131
FT /note="Sirohydrochlorin cobaltochelatase"
FT /id="PRO_1000046841"
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 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 131 AA; 14178 MW; D1B0688BFF4595F8 CRC64;
MSEKIGILAI GHGSRLPYNK EVVSEIAATI AKKHPDYVIK AGFMENTLPT VMEALADFDG
TGVTKIIAVP VFLASGVHIT EDIPEILKLD PETNEGKITV DGNEIPVTFG KPLGHHELLA
DLVFERAMEV M
