ID   COBS_GEOSW              Reviewed;         262 AA.
AC   C5D3K0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 59.
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=GWCH70_2206;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001638; ACS24915.1; -; Genomic_DNA.
DR   RefSeq; WP_015864336.1; NC_012793.1.
DR   AlphaFoldDB; C5D3K0; -.
DR   STRING; 471223.GWCH70_2206; -.
DR   EnsemblBacteria; ACS24915; ACS24915; GWCH70_2206.
DR   KEGG; gwc:GWCH70_2206; -.
DR   eggNOG; COG0368; Bacteria.
DR   HOGENOM; CLU_057426_1_2_9; -.
DR   OMA; GHTGDTY; -.
DR   OrthoDB; 1996371at2; -.
DR   UniPathway; UPA00148; UER00238.
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..262
FT                   /note="Adenosylcobinamide-GDP ribazoletransferase"
FT                   /id="PRO_1000212692"
FT   TRANSMEM        4..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        112..132
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        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
SQ   SEQUENCE   262 AA;  29484 MW;  29223AF211DBDF84 CRC64;
     MKAAWSGFLL SVQFLTVIPI RKQIDWNAAT ARWSVRAFPL VGALIGVIEA VTYFIFSSFS
     SLSPLFLALS LMWLSIWIAG GLHADGWMDV SDAFFSYRDI KRRQEIMSDS RVGAFAVLSI
     LCLLSFRFLF VFETIRSHLD IFLISVIPLL SRTAMAWLLI YGKPAKQTGM AAAFREHADR
     YDAHVAMIIG NCLLACLCAI HFSVWKTVIF LACGTIFAVF VARLFFEKQF GGITGDALGA
     FVEGVETWLW CMIWLLRSYV MV