CFBA_METJA
ID CFBA_METJA Reviewed; 143 AA.
AC Q58380;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=MJ0970;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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}.
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; L77117; AAB98975.1; -; Genomic_DNA.
DR PIR; B64421; B64421.
DR RefSeq; WP_010870484.1; NC_000909.1.
DR PDB; 6M25; X-ray; 2.50 A; A/B=1-143.
DR PDB; 6M26; X-ray; 2.61 A; A/B=1-143.
DR PDB; 6M27; X-ray; 2.60 A; A/B=1-143.
DR PDB; 6M28; X-ray; 3.00 A; A/B=1-143.
DR PDB; 6M29; X-ray; 2.90 A; A/B=1-143.
DR PDB; 6M2A; X-ray; 2.23 A; A/B=1-86, A/B=119-143.
DR PDB; 6M2E; X-ray; 2.60 A; A/B=1-143.
DR PDB; 6M2F; X-ray; 2.40 A; A/B=1-143.
DR PDB; 6M2G; X-ray; 2.80 A; A/B=1-143.
DR PDB; 6M2H; X-ray; 3.10 A; A/B=1-143.
DR PDBsum; 6M25; -.
DR PDBsum; 6M26; -.
DR PDBsum; 6M27; -.
DR PDBsum; 6M28; -.
DR PDBsum; 6M29; -.
DR PDBsum; 6M2A; -.
DR PDBsum; 6M2E; -.
DR PDBsum; 6M2F; -.
DR PDBsum; 6M2G; -.
DR PDBsum; 6M2H; -.
DR AlphaFoldDB; Q58380; -.
DR SMR; Q58380; -.
DR STRING; 243232.MJ_0970; -.
DR PRIDE; Q58380; -.
DR EnsemblBacteria; AAB98975; AAB98975; MJ_0970.
DR GeneID; 1451868; -.
DR KEGG; mja:MJ_0970; -.
DR eggNOG; arCOG02246; Archaea.
DR HOGENOM; CLU_065901_2_1_2; -.
DR InParanoid; Q58380; -.
DR OMA; HEHEKLE; -.
DR OrthoDB; 93992at2157; -.
DR PhylomeDB; Q58380; -.
DR UniPathway; UPA00148; UER00223.
DR Proteomes; UP000000805; 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 3D-structure; Cobalamin biosynthesis; Cobalt; Lyase; Metal-binding;
KW Methanogenesis; Nickel; Reference proteome.
FT CHAIN 1..143
FT /note="Sirohydrochlorin cobaltochelatase"
FT /id="PRO_0000150356"
FT ACT_SITE 9
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 9
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 9
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 70..75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 75
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 75
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:6M2A"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6M2F"
FT HELIX 15..30
FT /evidence="ECO:0007829|PDB:6M2A"
FT STRAND 34..46
FT /evidence="ECO:0007829|PDB:6M2A"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:6M2A"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:6M2A"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:6M2A"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:6M2A"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6M2A"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:6M2A"
SQ SEQUENCE 143 AA; 16519 MW; 3B2947A443F25098 CRC64;
MEALVLVGHG SRLPYSKELL VKLAEKVKER NLFPIVEIGL MEFSEPTIPQ AVKKAIEQGA
KRIIVVPVFL AHGIHTTRDI PRLLGLIEDN HEHHHEHSHH HHHHHHHEHE KLEIPEDVEI
IYREPIGADD RIVDIIIDRA FGR
