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CBIX_HALSA
ID   CBIX_HALSA              Reviewed;         292 AA.
AC   Q9HQM3;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Probable sirohydrochlorin cobaltochelatase;
DE            EC=4.99.1.3;
DE   AltName: Full=CbiXS;
GN   Name=cbiX; OrderedLocusNames=VNG_1093C;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
CC   -!- FUNCTION: Catalyzes the insertion of Co(2+) into sirohydrochlorin as
CC       part of the anaerobic pathway to cobalamin biosynthesis. {ECO:0000250}.
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   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 1/10.
CC   -!- DOMAIN: Seems to consist of two fused copies of the CbiX domain,
CC       resembling CbiK arrangement.
CC   -!- SIMILARITY: Belongs to the CbiX family. CbiXS subfamily. {ECO:0000305}.
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DR   EMBL; AE004437; AAG19490.1; -; Genomic_DNA.
DR   PIR; F84265; F84265.
DR   RefSeq; WP_010902785.1; NC_002607.1.
DR   AlphaFoldDB; Q9HQM3; -.
DR   SMR; Q9HQM3; -.
DR   STRING; 64091.VNG_1093C; -.
DR   PaxDb; Q9HQM3; -.
DR   EnsemblBacteria; AAG19490; AAG19490; VNG_1093C.
DR   GeneID; 5952827; -.
DR   GeneID; 62884462; -.
DR   KEGG; hal:VNG_1093C; -.
DR   PATRIC; fig|64091.14.peg.836; -.
DR   HOGENOM; CLU_096061_0_0_2; -.
DR   InParanoid; Q9HQM3; -.
DR   OMA; GYHTQED; -.
DR   OrthoDB; 42414at2157; -.
DR   PhylomeDB; Q9HQM3; -.
DR   UniPathway; UPA00148; UER00223.
DR   Proteomes; UP000000554; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016852; F:sirohydrochlorin cobaltochelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002762; CbiX-like.
DR   Pfam; PF01903; CbiX; 2.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Cobalt; Lyase; Metal-binding; Reference proteome;
KW   Repeat.
FT   CHAIN           1..292
FT                   /note="Probable sirohydrochlorin cobaltochelatase"
FT                   /id="PRO_0000150364"
FT   REGION          1..141
FT                   /note="CbiX 1"
FT   REGION          142..292
FT                   /note="CbiX 2"
FT   BINDING         152
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   292 AA;  31985 MW;  CF9C115BF1FDA2FF CRC64;
     MQALVIVGHG SHLNPGSSEP AYTHADTIRE SGAFDEVREA FWKEEPSFRN VLRTLESDEV
     YVVPLFISEG YFTEQVIPRE LRLDDFDPDD WDSDGTDADH VTLEADDVEK TIHYCGPVGT
     HDSMSEVIVQ RASSVTGREE FGDDFGLAVV GHGTERNENS AKAIYYHADQ IREMGVFGEV
     QAVFMDEDPE VDDVTDFFDT DDIVVVPLFV SDGFHTQEDI PEDMGLTDDY RTGYDIPTAV
     DGHDIWYSGA VGTEPLAADV VLERAADAGA PVGDAVDAVR EQTRGANAAA GD
 
 
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