ID   CBIX_SYNY3              Reviewed;         336 AA.
AC   Q55451;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Sirohydrochlorin cobaltochelatase;
DE            EC=4.99.1.3;
DE   AltName: Full=CbiXL;
GN   Name=cbiX; OrderedLocusNames=sll0037;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [3]
RP   CHARACTERIZATION OF IRON-SULFUR CLUSTER.
RX   PubMed=12917443; DOI=10.1074/jbc.m306112200;
RA   Leech H.K., Raux E., McLean K.J., Munro A.W., Robinson N.J.,
RA   Borrelly G.P.M., Malten M., Jahn D., Rigby S.E.J., Heathcote P.,
RA   Warren M.J.;
RT   "Characterization of the cobaltochelatase CbiXL: evidence for a 4Fe-4S
RT   center housed within an MXCXXC motif.";
RL   J. Biol. Chem. 278:41900-41907(2003).
CC   -!- FUNCTION: Chelates cobalt to the cobalamin precursor as part of the
CC       anaerobic pathway to cobalamin biosynthesis.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000305};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 1/10.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CbiX family. CbiXL subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA10794.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000022; BAA10794.1; ALT_INIT; Genomic_DNA.
DR   PIR; S75947; S75947.
DR   AlphaFoldDB; Q55451; -.
DR   SMR; Q55451; -.
DR   STRING; 1148.1001307; -.
DR   PaxDb; Q55451; -.
DR   EnsemblBacteria; BAA10794; BAA10794; BAA10794.
DR   KEGG; syn:sll0037; -.
DR   eggNOG; COG2138; Bacteria.
DR   InParanoid; Q55451; -.
DR   OMA; WCAVRPA; -.
DR   PhylomeDB; Q55451; -.
DR   UniPathway; UPA00148; UER00223.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   4Fe-4S; Cobalamin biosynthesis; Cobalt; Iron; Iron-sulfur; Lyase;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..336
FT                   /note="Sirohydrochlorin cobaltochelatase"
FT                   /id="PRO_0000150352"
FT   REGION          296..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         32
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000305"
FT   BINDING         285
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   336 AA;  38340 MW;  70981BD77DBAC4B9 CRC64;
     MTLTSVPAPV SLFPELELPP LPYHRPLLMI GHGTRDEDGR QTFLDFVAQY QALDHSRPVI
     PCFLELTEPN IQAGVQQCVD QGFEEISALP ILLFAARHNK FDVTNELDRS RQAHPQINFF
     YGRHFGITPA ILDLWKARLN QLDSPEANPQ GIDRQDTVLL FVGRGSSDPD ANGDVYKMAR
     MLWEGSGYQT VETCFIGISH PRLEEGFRRA RLYQPKRIIV LPYFLFMGAL VKKIFTITEE
     QRATFPEIEI QSLSEMGIQP ELLALVRERE IETQLGQVAM NCEACKFRLA FKNQGHGHDH
     GHGHHHHGHD HGHSHGEWVD TYIEPTAYHE KIWQAP