ID   CBIC_LEPIN              Reviewed;         220 AA.
AC   Q8EXP7;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Cobalt-precorrin-8 methylmutase;
DE            EC=5.4.99.60;
DE   AltName: Full=Cobalt-precorrin isomerase;
GN   Name=cbiC; OrderedLocusNames=LB_161;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), AND SUBUNIT.
RX   PubMed=16427313; DOI=10.1016/j.jsb.2005.11.011;
RA   Xue Y., Wei Z., Li X., Gong W.;
RT   "The crystal structure of putative precorrin isomerase CbiC in cobalamin
RT   biosynthesis.";
RL   J. Struct. Biol. 153:307-311(2006).
CC   -!- FUNCTION: Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-8X = cob(II)yrinate; Xref=Rhea:RHEA:16209,
CC         ChEBI:CHEBI:58894, ChEBI:CHEBI:70792; EC=5.4.99.60;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 9/10.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16427313}.
CC   -!- SIMILARITY: Belongs to the CobH/CbiC family. {ECO:0000305}.
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DR   EMBL; AE010301; AAN51720.2; -; Genomic_DNA.
DR   RefSeq; NP_714705.2; NC_004343.2.
DR   PDB; 2AFR; X-ray; 2.30 A; A=1-220.
DR   PDB; 2AFV; X-ray; 3.00 A; A/B=1-220.
DR   PDBsum; 2AFR; -.
DR   PDBsum; 2AFV; -.
DR   AlphaFoldDB; Q8EXP7; -.
DR   SMR; Q8EXP7; -.
DR   STRING; 189518.LB_161; -.
DR   EnsemblBacteria; AAN51720; AAN51720; LB_161.
DR   KEGG; lil:LB_161; -.
DR   PATRIC; fig|189518.3.peg.4489; -.
DR   HOGENOM; CLU_084703_1_1_12; -.
DR   InParanoid; Q8EXP7; -.
DR   BRENDA; 5.4.99.60; 2986.
DR   UniPathway; UPA00148; UER00230.
DR   EvolutionaryTrace; Q8EXP7; -.
DR   Proteomes; UP000001408; Chromosome II.
DR   GO; GO:0043778; F:cobalt-precorrin-8 methylmutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016993; F:precorrin-8X methylmutase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.10230; -; 1.
DR   InterPro; IPR003722; Cbl_synth_CobH/CbiC.
DR   InterPro; IPR036588; CobH/CbiC_sf.
DR   Pfam; PF02570; CbiC; 1.
DR   SUPFAM; SSF63965; SSF63965; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cobalamin biosynthesis; Isomerase; Reference proteome.
FT   CHAIN           1..220
FT                   /note="Cobalt-precorrin-8 methylmutase"
FT                   /id="PRO_0000430345"
FT   ACT_SITE        41
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   HELIX           6..23
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   HELIX           30..43
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   HELIX           48..51
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   HELIX           58..67
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   STRAND          71..76
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   HELIX           77..80
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   HELIX           85..89
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   HELIX           102..110
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   HELIX           115..125
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   HELIX           140..153
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   STRAND          158..162
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   HELIX           170..182
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   STRAND          190..193
FT                   /evidence="ECO:0007829|PDB:2AFR"
FT   HELIX           200..216
FT                   /evidence="ECO:0007829|PDB:2AFR"
SQ   SEQUENCE   220 AA;  24424 MW;  61BB8D07D57D434A CRC64;
     MRQITNLGRN IENKSFSIID EEAGPHSFAQ EEWEVVRRII HATADFDYKN ITKIHPQAID
     SGIQALKKGC PIVCDVQMIL SGLNPERLKV YGCKTYCFIS DEDVIENAKR KNSTRAIESI
     QKANSFNLLN ESIIVIGNAP TALLEIEKLI RQEGIKPALI VGVPVGFVSA KESKESILKL
     EYYNVTSIPY ILTMGRKGGS TIAVAILHAL LLLSSKRGER