CFBA_METAC
ID CFBA_METAC Reviewed; 130 AA.
AC Q8TJZ5;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
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, ECO:0000303|PubMed:27846569};
DE EC=4.99.1.11 {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000269|PubMed:27846569};
GN Name=cbiX {ECO:0000255|HAMAP-Rule:MF_00785};
GN Synonyms=cfbA {ECO:0000255|HAMAP-Rule:MF_00785,
GN ECO:0000303|PubMed:27846569};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
RN [2]
RP FUNCTION AS A SIROHYDROCHLORIN NICKELCHELATASE, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=27846569; DOI=10.1126/science.aag2947;
RA Zheng K., Ngo P.D., Owens V.L., Yang X.P., Mansoorabadi S.O.;
RT "The biosynthetic pathway of coenzyme F430 in methanogenic and
RT methanotrophic archaea.";
RL Science 354:339-342(2016).
CC -!- FUNCTION: Catalyzes the insertion of Co(2+) into sirohydrochlorin as
CC part of the anaerobic pathway to cobalamin biosynthesis (Potential).
CC Involved in the biosynthesis of the unique nickel-containing
CC tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M
CC reductase (MCR), which plays a key role in methanogenesis and anaerobic
CC methane oxidation (PubMed:27846569). Catalyzes the insertion of Ni(2+)
CC into sirohydrochlorin to yield Ni-sirohydrochlorin (PubMed:27846569).
CC {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000269|PubMed:27846569}.
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 ECO:0000269|PubMed:27846569};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE010299; AAM06986.1; -; Genomic_DNA.
DR RefSeq; WP_011023539.1; NC_003552.1.
DR AlphaFoldDB; Q8TJZ5; -.
DR SMR; Q8TJZ5; -.
DR STRING; 188937.MA_3631; -.
DR EnsemblBacteria; AAM06986; AAM06986; MA_3631.
DR GeneID; 1475524; -.
DR KEGG; mac:MA_3631; -.
DR HOGENOM; CLU_065901_2_1_2; -.
DR InParanoid; Q8TJZ5; -.
DR OMA; HEHEKLE; -.
DR OrthoDB; 93992at2157; -.
DR PhylomeDB; Q8TJZ5; -.
DR BioCyc; MetaCyc:MON-20113; -.
DR UniPathway; UPA00148; UER00223.
DR Proteomes; UP000002487; 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 1: Evidence at protein level;
KW Cobalamin biosynthesis; Cobalt; Lyase; Metal-binding; Methanogenesis;
KW Nickel; Reference proteome.
FT CHAIN 1..130
FT /note="Sirohydrochlorin cobaltochelatase"
FT /id="PRO_0000150354"
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; 13746 MW; 613F91A41367DDB0 CRC64;
MTEKLGILAI GHGSKLPYNK EVVSQIADYI AQKHSDVVVR AGFMENSEPT LEEAIAGFAG
TGVTKIAAVP VFLASGVHIT KDIPGILSLD EKGCGILNID GKDVPLCYAK PLGADELIAD
LVFKRVQEAL
