ID   CBIX_PRIMG              Reviewed;         306 AA.
AC   O87690;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Sirohydrochlorin cobaltochelatase;
DE            EC=4.99.1.3;
DE   AltName: Full=CbiXL;
GN   Name=cbiX;
OS   Priestia megaterium (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 509 / CCM 1464 / NBRC 12109;
RX   PubMed=9742225; DOI=10.1042/bj3350159;
RA   Raux E., Lanois A., Warren M.J., Rambach A., Thermes C.;
RT   "Cobalamin (vitamin B12) biosynthesis: identification and characterization
RT   of a Bacillus megaterium cobI operon.";
RL   Biochem. J. 335:159-166(1998).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=DSM 509 / CCM 1464 / NBRC 12109;
RX   PubMed=12408752; DOI=10.1042/bj20021443;
RA   Raux E., Leech H.K., Beck R., Schubert H.L., Santander P.J., Roessner C.A.,
RA   Scott A.I., Martens J.H., Jahn D., Thermes C., Rambach A., Warren M.J.;
RT   "Identification and functional analysis of enzymes required for precorrin-2
RT   dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and
RT   cobalamin in Bacillus megaterium.";
RL   Biochem. J. 370:505-516(2003).
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}.
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DR   EMBL; AJ000758; CAA04308.1; -; Genomic_DNA.
DR   PIR; T44684; T44684.
DR   AlphaFoldDB; O87690; -.
DR   SMR; O87690; -.
DR   BioCyc; MetaCyc:MON-14879; -.
DR   UniPathway; UPA00148; UER00223.
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.
FT   CHAIN           1..306
FT                   /note="Sirohydrochlorin cobaltochelatase"
FT                   /id="PRO_0000150351"
FT   REGION          276..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..295
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         14
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
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         262
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   306 AA;  34882 MW;  D628CCEDD89368F7 CRC64;
     MGGHYMKSVL FVGHGSRDPE GNDREFISTM KHDWDASILV ETCFLEFERP NVSQGIDTCV
     AKGAQDVVVI PIMLLPAGHS KIHIPAAIDE AKEKYPHVNF VYGRPIGVHE EALEILKTRL
     QESGENLETP AEDTAVIVLG RGGSDPDANS DLYKITRLLW EKTNYKIVET SFMGVTAPLI
     DEGVERCLKL GAKKVVILPY FLFTGVLIKR LEEMVKQYKM QHENIEFKLA GYFGFHPKLQ
     TILKERAEEG LEGEVKMNCD TCQYRLGIME HIDHHHHHDH DHDHDHGHHH HDHHHDHHED
     KVGELK