ID   A0A378GEI3_9ENTR        Unreviewed;       259 AA.
AC   A0A378GEI3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   14-DEC-2022, entry version 11.
DE   RecName: Full=Sirohydrochlorin cobaltochelatase {ECO:0000256|PIRNR:PIRNR033579};
DE            EC=4.99.1.3 {ECO:0000256|PIRNR:PIRNR033579};
GN   Name=cbiK {ECO:0000313|EMBL:STW97593.1};
GN   ORFNames=NCTC9737_01037 {ECO:0000313|EMBL:STW97593.1};
OS   Kluyvera ascorbata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Kluyvera.
OX   NCBI_TaxID=51288 {ECO:0000313|EMBL:STW97593.1, ECO:0000313|Proteomes:UP000255427};
RN   [1] {ECO:0000313|EMBL:STW97593.1, ECO:0000313|Proteomes:UP000255427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC9737 {ECO:0000313|EMBL:STW97593.1,
RC   ECO:0000313|Proteomes:UP000255427};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the insertion of Co(2+) into sirohydrochlorin.
CC       {ECO:0000256|PIRNR:PIRNR033579}.
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:0000256|PIRNR:PIRNR033579};
CC   -!- SIMILARITY: Belongs to the CbiK family.
CC       {ECO:0000256|PIRNR:PIRNR033579}.
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DR   EMBL; UGNM01000001; STW97593.1; -; Genomic_DNA.
DR   RefSeq; WP_035895324.1; NZ_UGNM01000001.1.
DR   AlphaFoldDB; A0A378GEI3; -.
DR   EnsemblBacteria; STW97593; STW97593; NCTC9737_01037.
DR   Proteomes; UP000255427; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016852; F:sirohydrochlorin cobaltochelatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019251; P:anaerobic cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR   InterPro; IPR010388; Anaerobic_Co-chelatase.
DR   Pfam; PF06180; CbiK; 1.
DR   PIRSF; PIRSF033579; Anaer_Co_chel; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|PIRSR:PIRSR033579-3};
KW   Lyase {ECO:0000256|PIRNR:PIRNR033579, ECO:0000313|EMBL:STW97593.1};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR033579,
KW   ECO:0000256|PIRSR:PIRSR033579-3}.
FT   ACT_SITE        145
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR033579-1"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR033579-2"
FT   BINDING         85..92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR033579-2"
FT   BINDING         145
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR033579-3"
FT   BINDING         175
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR033579-3"
FT   BINDING         202..203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR033579-2"
FT   BINDING         207
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR033579-3"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR033579-2"
SQ   SEQUENCE   259 AA;  28458 MW;  D926B2697AEAD632 CRC64;
     MKKALLVVSF GTSYHDTCEK NIVACERELA ASCPDRDLFR AFTSGMIIRK LKARDGIDTD
     TPLEALQKLA DLGYDDVAVQ SLHIINGDEY EKIAREVQSL RPLFKRLTLG TPLLSGHDDY
     VRLMEALTQQ MPALKANEKV VFMGHGASHH AFAAYACLDH MMTAQRFPAR VGAVESYPEV
     EVLIESMSKE GVSAVHLMPL MLVAGDHAIN DMASDEDDSW KTLFNAAGIP ATPWLCGLGE
     NPVVRAMFVA HLQQSLEAA
//