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COBS_CHLTE
ID   COBS_CHLTE              Reviewed;         254 AA.
AC   Q8KDU6;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2003, sequence version 2.
DT   25-MAY-2022, entry version 106.
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=CT0948;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM72183.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006470; AAM72183.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_661841.1; NC_002932.3.
DR   AlphaFoldDB; Q8KDU6; -.
DR   STRING; 194439.CT0948; -.
DR   EnsemblBacteria; AAM72183; AAM72183; CT0948.
DR   KEGG; cte:CT0948; -.
DR   PATRIC; fig|194439.7.peg.859; -.
DR   eggNOG; COG0368; Bacteria.
DR   HOGENOM; CLU_057426_1_1_10; -.
DR   OMA; GHTGDTY; -.
DR   OrthoDB; 1996371at2; -.
DR   UniPathway; UPA00148; UER00238.
DR   Proteomes; UP000001007; 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 inner membrane; Cell membrane; Cobalamin biosynthesis; Magnesium;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..254
FT                   /note="Adenosylcobinamide-GDP ribazoletransferase"
FT                   /id="PRO_0000146869"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
SQ   SEQUENCE   254 AA;  26727 MW;  50FAAD9656531DC4 CRC64;
     MLSGLVTALR TLTALPVPGR DAERFSSSLY WFPVVGLVIG GIVVLLARAG MGVGWPELAA
     VLALLGGLIL TRGLHADGLA DLADGFFGGR TREAALRIMK DPNVGSFGSL ALIGVMLFKW
     ICLLELARAE AYGMIAAGAV LSRTAQVLLA ARMPYARSDG GTAMAFVEDA GWPHLLVASI
     SGVVLLFVLL DWQLAPSLIL LFGSVVALFF VGWLSHRKIG GITGDVLGAC SELVEAAVWL
     LAALWLKGLF WAIA
 
 
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