CBIG_SALTY
ID CBIG_SALTY Reviewed; 351 AA.
AC Q05631;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Cobalt-precorrin-5A hydrolase;
DE EC=3.7.1.12;
GN Name=cbiG; OrderedLocusNames=STM2028;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=8501034; DOI=10.1128/jb.175.11.3303-3316.1993;
RA Roth J.R., Lawrence J.G., Rubenfield M., Kieffer-Higgins S., Church G.M.;
RT "Characterization of the cobalamin (vitamin B12) biosynthetic genes of
RT Salmonella typhimurium.";
RL J. Bacteriol. 175:3303-3316(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION.
RX PubMed=16866557; DOI=10.1021/ja062940a;
RA Kajiwara Y., Santander P.J., Roessner C.A., Perez L.M., Scott A.I.;
RT "Genetically engineered synthesis and structural characterization of
RT cobalt-precorrin 5A and -5B, two new intermediates on the anaerobic pathway
RT to vitamin B12: definition of the roles of the CbiF and CbiG enzymes.";
RL J. Am. Chem. Soc. 128:9971-9978(2006).
CC -!- FUNCTION: Catalyzes the hydrolysis of the ring A acetate delta-lactone
CC of cobalt-precorrin-5A resulting in the loss of the C-20 carbon and its
CC attached methyl group in the form of acetaldehyde.
CC {ECO:0000269|PubMed:16866557}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co-precorrin-5A + H2O = acetaldehyde + Co-precorrin-5B + H(+);
CC Xref=Rhea:RHEA:26281, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:60062, ChEBI:CHEBI:60063; EC=3.7.1.12;
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC step 5/10.
CC -!- SIMILARITY: Belongs to the CbiG family. {ECO:0000305}.
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DR EMBL; L12006; AAA27259.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20932.1; -; Genomic_DNA.
DR RefSeq; NP_460973.1; NC_003197.2.
DR RefSeq; WP_001098914.1; NC_003197.2.
DR AlphaFoldDB; Q05631; -.
DR SMR; Q05631; -.
DR STRING; 99287.STM2028; -.
DR PaxDb; Q05631; -.
DR DNASU; 1253549; -.
DR EnsemblBacteria; AAL20932; AAL20932; STM2028.
DR GeneID; 1253549; -.
DR KEGG; stm:STM2028; -.
DR PATRIC; fig|99287.12.peg.2150; -.
DR HOGENOM; CLU_028397_0_0_6; -.
DR OMA; GIGCNRG; -.
DR PhylomeDB; Q05631; -.
DR BioCyc; MetaCyc:MON-13219; -.
DR BioCyc; SENT99287:STM2028-MON; -.
DR UniPathway; UPA00148; UER00561.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0043779; F:cobalt-precorrin-5A acetaldehyde-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.420.180; -; 1.
DR InterPro; IPR021745; CbiG_mid.
DR InterPro; IPR021744; CbiG_N.
DR InterPro; IPR002750; CobE/GbiG_C.
DR InterPro; IPR036518; CobE/GbiG_C_sf.
DR InterPro; IPR038029; GbiG_N_sf.
DR Pfam; PF01890; CbiG_C; 1.
DR Pfam; PF11761; CbiG_mid; 1.
DR Pfam; PF11760; CbiG_N; 1.
DR SUPFAM; SSF159664; SSF159664; 1.
DR SUPFAM; SSF159672; SSF159672; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Hydrolase; Reference proteome.
FT CHAIN 1..351
FT /note="Cobalt-precorrin-5A hydrolase"
FT /id="PRO_0000089373"
SQ SEQUENCE 351 AA; 37783 MW; 6C7323E15B3F1567 CRC64;
MNTVKPESIA LFCLTPGGVA LAKRLAAMLP LTCFTSEKLR EEGFIPFDGG FANTARQAFT
TYTALIFIGA TGIAVRVLAP LVNDKFSDPA VVVIDERGQH VISLLSGHAG GANALTRYLA
GMLGADPVIT TATDVNEMSA LDTLAFQLNA RMSDLRTAVK TVNQMLVSHQ RVGLWWDAEL
TEEIGQCDIR GFIPVDDLQR LPELDALICV SLRNDLPELP VPHWKLVPQR VVAGIGCRRD
TPFPLLATLL ARQLEAQKLD PLALKAIGSV TLKKGEPGLI QLASCCRVPF KTFTAEALRE
FEHHFPGSGF VRKTVGVGSV SGPAAWLLSQ GQLLGETLRE QGVTITLGVA H