ID   COBS_PICTO              Reviewed;         241 AA.
AC   Q6L174;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=PTO0693;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017261; AAT43278.1; -; Genomic_DNA.
DR   RefSeq; WP_011177494.1; NC_005877.1.
DR   AlphaFoldDB; Q6L174; -.
DR   STRING; 263820.PTO0693; -.
DR   EnsemblBacteria; AAT43278; AAT43278; PTO0693.
DR   GeneID; 2845050; -.
DR   KEGG; pto:PTO0693; -.
DR   eggNOG; arCOG04338; Archaea.
DR   HOGENOM; CLU_057426_2_0_2; -.
DR   OMA; CACCGIP; -.
DR   OrthoDB; 108934at2157; -.
DR   UniPathway; UPA00148; UER00238.
DR   Proteomes; UP000000438; 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;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..241
FT                   /note="Adenosylcobinamide-GDP ribazoletransferase"
FT                   /id="PRO_0000146914"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
SQ   SEQUENCE   241 AA;  27136 MW;  92FCA5CCDC6ED98C CRC64;
     MQGLKSAISF FTIIPVKADL NKNIVFFFTI TGAITGLMAA SIFYLTSFIN QLLASVASVS
     FLIIIYGFNH ADAVLDLGDT FMVHDPEKKK IIIKDVYHGT GSVVTFFIIY IITISLLSSF
     NSIQGSIALI LSETISRFSM LMSMYKSNSF SGGISEIFIS YFDKPFKITF FNFLVIILIF
     LIFYKYIIFT MFSLISIVIS YYFKSHEQKI FNGINGDIIG FTGELSRLIS LLLILISFKL
     I