CFBA_METBF
ID CFBA_METBF Reviewed; 130 AA.
AC P61816; Q46FL4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Sirohydrochlorin cobaltochelatase {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000303|PubMed:12686546};
DE EC=4.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000269|PubMed:12686546};
DE AltName: Full=CbiXS {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000303|PubMed:12686546};
DE AltName: Full=Sirohydrochlorin nickelchelatase {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000303|PubMed:28225763};
DE EC=4.99.1.11 {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000269|PubMed:28225763};
GN Name=cbiX {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000303|PubMed:12686546};
GN Synonyms=cfbA {ECO:0000255|HAMAP-Rule:MF_00785,
GN ECO:0000303|PubMed:28225763};
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
RN [2]
RP FUNCTION AS A SIROHYDROCHLORIN COBALTOCHELATASE, CATALYTIC ACTIVITY,
RP PATHWAY, AND SUBUNIT.
RX PubMed=12686546; DOI=10.1074/jbc.m302468200;
RA Brindley A.A., Raux E., Leech H.K., Schubert H.L., Warren M.J.;
RT "A story of chelatase evolution: identification and characterization of a
RT small 13-15-kDa 'ancestral' cobaltochelatase (CbiXS) in the archaea.";
RL J. Biol. Chem. 278:22388-22395(2003).
RN [3]
RP FUNCTION AS A SIROHYDROCHLORIN NICKELCHELATASE, AND CATALYTIC ACTIVITY.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=28225763; DOI=10.1038/nature21427;
RA Moore S.J., Sowa S.T., Schuchardt C., Deery E., Lawrence A.D., Ramos J.V.,
RA Billig S., Birkemeyer C., Chivers P.T., Howard M.J., Rigby S.E., Layer G.,
RA Warren M.J.;
RT "Elucidation of the biosynthesis of the methane catalyst coenzyme F430.";
RL Nature 543:78-82(2017).
CC -!- FUNCTION: Catalyzes the insertion of Co(2+) into sirohydrochlorin as
CC part of the anaerobic pathway to cobalamin biosynthesis
CC (PubMed:12686546). Involved in the biosynthesis of the unique nickel-
CC containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-
CC coenzyme M reductase (MCR), which plays a key role in methanogenesis
CC and anaerobic methane oxidation (PubMed:28225763). Catalyzes the
CC insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin
CC (PubMed:28225763). {ECO:0000255|HAMAP-Rule:MF_00785,
CC ECO:0000269|PubMed:12686546, ECO:0000269|PubMed:28225763}.
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 ECO:0000269|PubMed:12686546};
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:28225763};
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 ECO:0000269|PubMed:12686546}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00785, ECO:0000305|PubMed:12686546}.
CC -!- SIMILARITY: Belongs to the CbiX family. CbiXS subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00785}.
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DR EMBL; CP000099; AAZ69328.1; -; Genomic_DNA.
DR RefSeq; WP_011305381.1; NC_007355.1.
DR PDB; 6M2A; X-ray; 2.23 A; A/B=90-104.
DR PDBsum; 6M2A; -.
DR AlphaFoldDB; P61816; -.
DR SMR; P61816; -.
DR STRING; 269797.Mbar_A0344; -.
DR EnsemblBacteria; AAZ69328; AAZ69328; Mbar_A0344.
DR GeneID; 3626588; -.
DR KEGG; mba:Mbar_A0344; -.
DR eggNOG; arCOG02246; Archaea.
DR HOGENOM; CLU_065901_2_1_2; -.
DR OMA; HEHEKLE; -.
DR OrthoDB; 93992at2157; -.
DR BRENDA; 4.99.1.3; 3250.
DR UniPathway; UPA00148; UER00223.
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 3D-structure; Cobalamin biosynthesis; Cobalt; Lyase; Metal-binding;
KW Methanogenesis; Nickel.
FT CHAIN 1..130
FT /note="Sirohydrochlorin cobaltochelatase"
FT /id="PRO_0000150355"
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"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6M2A"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6M2A"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6M2A"
SQ SEQUENCE 130 AA; 13850 MW; CA3889CF8B6E8D8C CRC64;
MTEKLGILAI GHGSKLPYNK EVVTQIADYI ARKHSDVVVR AGFMENSEPT LGEAIEGFSG
TGVTKIAAVP VFLASGVHIT KDIPRILSLD ENGCGTLEID GKTVPLCYAN PLGADELIAD
LVFKRVQEAL
