COBS_SALTY
ID COBS_SALTY Reviewed; 247 AA.
AC Q05602;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Adenosylcobinamide-GDP ribazoletransferase;
DE EC=2.7.8.26;
DE AltName: Full=Cobalamin synthase;
DE AltName: Full=Cobalamin-5'-phosphate synthase;
GN Name=cobS; OrderedLocusNames=STM2017;
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, AND CATALYTIC ACTIVITY.
RC STRAIN=LT2 / TR6583 / SA2929;
RX PubMed=10518530; DOI=10.1073/pnas.96.21.11798;
RA Maggio-Hall L.A., Escalante-Semerena J.C.;
RT "In vitro synthesis of the nucleotide loop of cobalamin by Salmonella
RT typhimurium enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11798-11803(1999).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=LT2 / TR6583 / SA2929;
RX PubMed=15133100; DOI=10.1099/mic.0.26952-0;
RA Maggio-Hall L.A., Claas K.R., Escalante-Semerena J.C.;
RT "The last step in coenzyme B(12) synthesis is localized to the cell
RT membrane in bacteria and archaea.";
RL Microbiology 150:1385-1395(2004).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17209023; DOI=10.1128/jb.01665-06;
RA Zayas C.L., Escalante-Semerena J.C.;
RT "Reassessment of the late steps of coenzyme B12 synthesis in Salmonella
RT enterica: evidence that dephosphorylation of adenosylcobalamin-5'-phosphate
RT by the CobC phosphatase is the last step of the pathway.";
RL J. Bacteriol. 189:2210-2218(2007).
CC -!- FUNCTION: Joins adenosylcobinamide-GDP and alpha-ribazole to generate
CC adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin
CC 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-
CC phosphate. {ECO:0000269|PubMed:10518530, ECO:0000269|PubMed:17209023}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosylcob(III)inamide-GDP + alpha-ribazole =
CC adenosylcob(III)alamin + GMP + H(+); Xref=Rhea:RHEA:16049,
CC ChEBI:CHEBI:10329, ChEBI:CHEBI:15378, ChEBI:CHEBI:18408,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:60487; EC=2.7.8.26;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate =
CC adenosylcob(III)alamin 5'-phosphate + GMP + H(+);
CC Xref=Rhea:RHEA:23560, ChEBI:CHEBI:15378, ChEBI:CHEBI:57918,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:60487, ChEBI:CHEBI:60493; EC=2.7.8.26;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15133100}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15133100}.
CC -!- SIMILARITY: Belongs to the CobS family. {ECO:0000305}.
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DR EMBL; L12006; AAA27270.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20921.1; -; Genomic_DNA.
DR RefSeq; NP_460962.1; NC_003197.2.
DR RefSeq; WP_000039997.1; NC_003197.2.
DR AlphaFoldDB; Q05602; -.
DR STRING; 99287.STM2017; -.
DR PaxDb; Q05602; -.
DR EnsemblBacteria; AAL20921; AAL20921; STM2017.
DR GeneID; 1253538; -.
DR KEGG; stm:STM2017; -.
DR PATRIC; fig|99287.12.peg.2139; -.
DR HOGENOM; CLU_057426_3_1_6; -.
DR OMA; GHTGDTY; -.
DR PhylomeDB; Q05602; -.
DR BioCyc; MetaCyc:MON-13212; -.
DR BioCyc; SENT99287:STM2017-MON; -.
DR UniPathway; UPA00148; UER00238.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051073; F:adenosylcobinamide-GDP ribazoletransferase activity; IBA:GO_Central.
DR GO; GO:0008818; F:cobalamin 5'-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_00719; CobS; 1.
DR InterPro; IPR003805; CobS.
DR PANTHER; PTHR34148; PTHR34148; 1.
DR Pfam; PF02654; CobS; 1.
DR TIGRFAMs; TIGR00317; cobS; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Cobalamin biosynthesis; Magnesium;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..247
FT /note="Adenosylcobinamide-GDP ribazoletransferase"
FT /id="PRO_0000146895"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 4
FT /note="L -> P (in Ref. 1; AAA27270)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="W -> R (in Ref. 1; AAA27270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 26316 MW; FBF4D5948A6E9A18 CRC64;
MSKLFWAMLA FISRLPVPSR WSQGLDFEQY SRGIVMFPFI GLILGGVSGL IFILLQPWCG
IPLAALFCIL ALALLTGGFH LDGLADTCDG IFSARRRERM LEIMRDSRLG THGGLALIFV
LLAKILVVSE LALRGTPMLA ALAAACAAGR GSAVLLMYRH RYAREEGLGN VFIGKVSGRQ
TCITLGLAVI VATVLLPGMQ GLAAMVVTCA AIFILGQLLK RTLGGQTGDT LGAAIELGEL
IFLLALL
