ID   COBS_LISW6              Reviewed;         248 AA.
AC   A0AHP2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=lwe1106;
OS   Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS   NCTC 11857 / SLCC 5334 / V8).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=386043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX   PubMed=16936040; DOI=10.1128/jb.00758-06;
RA   Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA   Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA   Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA   Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT   "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT   genome reduction with Listeria innocua as compared to Listeria
RT   monocytogenes.";
RL   J. Bacteriol. 188:7405-7415(2006).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00719};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00719}.
CC   -!- SIMILARITY: Belongs to the CobS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00719}.
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DR   EMBL; AM263198; CAK20524.1; -; Genomic_DNA.
DR   RefSeq; WP_011701925.1; NC_008555.1.
DR   AlphaFoldDB; A0AHP2; -.
DR   STRING; 386043.lwe1106; -.
DR   EnsemblBacteria; CAK20524; CAK20524; lwe1106.
DR   GeneID; 61188989; -.
DR   KEGG; lwe:lwe1106; -.
DR   eggNOG; COG0368; Bacteria.
DR   HOGENOM; CLU_057426_1_2_9; -.
DR   OMA; FMDSMDG; -.
DR   OrthoDB; 1996371at2; -.
DR   UniPathway; UPA00148; UER00238.
DR   Proteomes; UP000000779; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0008818; F:cobalamin 5'-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
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 membrane; Cobalamin biosynthesis; Magnesium; Membrane; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..248
FT                   /note="Adenosylcobinamide-GDP ribazoletransferase"
FT                   /id="PRO_1000045773"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
SQ   SEQUENCE   248 AA;  27138 MW;  93A6C01FC7019893 CRC64;
     MKTLILLIQF FTRIPIPIAI NMDEVNLKKG SALLPFVGLI IGAWNWLVFT LVALVMPLPV
     AIIAGLFAEI IITGGFHVDA LADTADGLFS SRKKERMLEI MKDSRVGANG VIAICFYFLF
     YGALFLSVPS AYEIGWLFFV LPIVAKGVTM LLFAKMTYAG SNEGLGSIFL GVPWWPIAIS
     QLFVLFILGL VFSYIGLLAY AGVILFTIIY RTFVYKRIGG MNGDTLGAGG QMGQLVCLFC
     LVLVWGLI