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Database: UniProt
Entry: G7V602_THELD
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ID   G7V602_THELD            Unreviewed;       308 AA.
AC   G7V602;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN   Name=cobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN   OrderedLocusNames=Tlie_0161 {ECO:0000313|EMBL:AER65907.1};
OS   Thermovirga lienii (strain ATCC BAA-1197 / DSM 17291 / Cas60314).
OC   Bacteria; Synergistota; Synergistia; Synergistales; Thermovirgaceae;
OC   Thermovirga.
OX   NCBI_TaxID=580340 {ECO:0000313|EMBL:AER65907.1, ECO:0000313|Proteomes:UP000005868};
RN   [1] {ECO:0000313|Proteomes:UP000005868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1197 / DSM 17291 / Cas60314
RC   {ECO:0000313|Proteomes:UP000005868};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Saunders E.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Last F.I., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.-M.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of chromosome of Thermovirga lienii DSM 17291.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AER65907.1, ECO:0000313|Proteomes:UP000005868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1197 / DSM 17291 / Cas60314
RC   {ECO:0000313|Proteomes:UP000005868};
RX   PubMed=22768366; DOI=10.4056/sigs.2726028;
RA   Goker M., Saunders E., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA   Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Chang Y.J., Jeffries C.D.,
RA   Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Genome sequence of the moderately thermophilic, amino-acid-degrading and
RT   sulfur-reducing bacterium Thermovirga lienii type strain (Cas60314(T)).";
RL   Stand. Genomic Sci. 6:230-239(2012).
CC   -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC       aminopropanol on the F carboxylic group. {ECO:0000256|HAMAP-
CC       Rule:MF_00024}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00024}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC       ECO:0000256|HAMAP-Rule:MF_00024}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|HAMAP-Rule:MF_00024}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CobD/CbiB family.
CC       {ECO:0000256|ARBA:ARBA00006263, ECO:0000256|HAMAP-Rule:MF_00024}.
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DR   EMBL; CP003096; AER65907.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7V602; -.
DR   STRING; 580340.Tlie_0161; -.
DR   KEGG; tli:Tlie_0161; -.
DR   eggNOG; COG1270; Bacteria.
DR   HOGENOM; CLU_054212_0_0_0; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000005868; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048472; F:threonine-phosphate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00024; CobD_CbiB; 1.
DR   InterPro; IPR004485; Cobalamin_biosynth_CobD/CbiB.
DR   NCBIfam; TIGR00380; cobal_cbiB; 1.
DR   PANTHER; PTHR34308; COBALAMIN BIOSYNTHESIS PROTEIN CBIB; 1.
DR   PANTHER; PTHR34308:SF1; COBALAMIN BIOSYNTHESIS PROTEIN CBIB; 1.
DR   Pfam; PF03186; CobD_Cbib; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00024};
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_00024};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005868};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00024};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00024}.
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        75..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        153..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        201..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        289..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
SQ   SEQUENCE   308 AA;  33564 MW;  5FF87329AB99573F CRC64;
     MAFAVDLVFG DPYGFPHPVR GIGWLVAKTE RFIRNRFTTA RGLKVSGTFM AFCVPALVWG
     VAFSVLEIAG FIHPLLYHLL NILMLYTTLS VKSLGYEVGK VHKALRKGDI VGAQKALSYL
     VSRETKDLDD QGIIRAAVET VAENTVDGVI SPLFYAFLGG APLAMCYKAI NTLDSMVGYK
     NEKYIHLGWA SARLDDLANF IPARLAGLII PLASGVCGFH MFNSFRIVLR DRRNHASPNA
     GFPEAAVAGA LGVQLGGEST YFGKKIKKPT LGDPMVPLEP KHIKAGIRIM YTAATIMVTA
     GFLISRWV
//
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