COBS_VIBCH
ID COBS_VIBCH Reviewed; 261 AA.
AC Q9KSL8;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Adenosylcobinamide-GDP ribazoletransferase {ECO:0000255|HAMAP-Rule:MF_00719};
DE EC=2.7.8.26 {ECO:0000255|HAMAP-Rule:MF_00719};
DE AltName: Full=Cobalamin synthase {ECO:0000255|HAMAP-Rule:MF_00719};
DE AltName: Full=Cobalamin-5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00719};
GN Name=cobS {ECO:0000255|HAMAP-Rule:MF_00719}; OrderedLocusNames=VC_1238;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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:0000255|HAMAP-Rule:MF_00719}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00719};
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00719};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00719};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
CC {ECO:0000255|HAMAP-Rule:MF_00719}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00719}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00719}.
CC -!- SIMILARITY: Belongs to the CobS family. {ECO:0000255|HAMAP-
CC Rule:MF_00719}.
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DR EMBL; AE003852; AAF94397.1; -; Genomic_DNA.
DR PIR; A82224; A82224.
DR RefSeq; NP_230883.1; NC_002505.1.
DR RefSeq; WP_000718969.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KSL8; -.
DR STRING; 243277.VC_1238; -.
DR DNASU; 2614675; -.
DR EnsemblBacteria; AAF94397; AAF94397; VC_1238.
DR GeneID; 57739909; -.
DR KEGG; vch:VC_1238; -.
DR PATRIC; fig|243277.26.peg.1180; -.
DR eggNOG; COG0368; Bacteria.
DR HOGENOM; CLU_057426_1_1_6; -.
DR OMA; FMDSMDG; -.
DR BioCyc; VCHO:VC1238-MON; -.
DR UniPathway; UPA00148; UER00238.
DR Proteomes; UP000000584; Chromosome 1.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cobalamin biosynthesis; Magnesium;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..261
FT /note="Adenosylcobinamide-GDP ribazoletransferase"
FT /id="PRO_0000146902"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
SQ SEQUENCE 261 AA; 28593 MW; E59B33A132A3364B CRC64;
MAAILRYQLE LFLLAVSFFS RIPVPVSLPY SSERMNQAGR YFALVGLLLG AICALVYSLA
TQLFSTNISV FLTMVLSLLL TGAFHEDGLA DMADGVGGGM TAERRLEIMK DSRIGTYGSS
ALIMVLLGKY LLLTELADLT SLVPVWLLAY TLSRAVAASL IRNTPYVSDT DSSKSKPLAQ
QLSGTDVAVL SLTALATLLY FSWQFIGVMI AASLIFRQIF RQWLIRRLGG FTGDCLGAAQ
QLMEILIYLI LLAFLQHEVM I
