CFBA_METTH
ID CFBA_METTH Reviewed; 143 AA.
AC O27448;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=MTH_1397;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, 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).
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 (Potential). Catalyzes the insertion of
CC Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin (Potential).
CC {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000269|PubMed:12686546}.
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 -!- 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:0000269|PubMed:12686546}.
CC -!- SIMILARITY: Belongs to the CbiX family. CbiXS subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85874.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000666; AAB85874.1; ALT_INIT; Genomic_DNA.
DR PIR; H69052; H69052.
DR RefSeq; WP_048061042.1; NC_000916.1.
DR AlphaFoldDB; O27448; -.
DR SMR; O27448; -.
DR STRING; 187420.MTH_1397; -.
DR EnsemblBacteria; AAB85874; AAB85874; MTH_1397.
DR GeneID; 24854511; -.
DR KEGG; mth:MTH_1397; -.
DR PATRIC; fig|187420.15.peg.1362; -.
DR HOGENOM; CLU_065901_2_1_2; -.
DR OMA; HEHEKLE; -.
DR UniPathway; UPA00148; UER00223.
DR Proteomes; UP000005223; 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..143
FT /note="Sirohydrochlorin cobaltochelatase"
FT /id="PRO_0000150360"
FT ACT_SITE 18
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 18
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 18
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 78..83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 83
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 83
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
SQ SEQUENCE 143 AA; 15826 MW; 76E2FBB16655B6A0 CRC64;
MDSNSNQKPK IGVLLVGHGS RLPYGEEVIN GIADIYRQEA DHPVAVGFMN MSRPSIPEAI
NELAAMGVEK IIVTPVFLAH GVHTKHDIPH ILGLDNGAEG HHHHEHEHEH EEFEFDGEIV
YTEPLGADPR IAEIIRDRVK SAI
