ID   COBD_STRSV              Reviewed;         316 AA.
AC   A3CL57;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000255|HAMAP-Rule:MF_00024};
GN   Name=cobD {ECO:0000255|HAMAP-Rule:MF_00024}; OrderedLocusNames=SSA_0464;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
CC   -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC       aminopropanol on the F carboxylic group. {ECO:0000255|HAMAP-
CC       Rule:MF_00024}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00024}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00024};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00024}.
CC   -!- SIMILARITY: Belongs to the CobD/CbiB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00024}.
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DR   EMBL; CP000387; ABN43912.1; -; Genomic_DNA.
DR   RefSeq; WP_002898268.1; NC_009009.1.
DR   RefSeq; YP_001034462.1; NC_009009.1.
DR   AlphaFoldDB; A3CL57; -.
DR   STRING; 388919.SSA_0464; -.
DR   EnsemblBacteria; ABN43912; ABN43912; SSA_0464.
DR   KEGG; ssa:SSA_0464; -.
DR   PATRIC; fig|388919.9.peg.448; -.
DR   eggNOG; COG1270; Bacteria.
DR   HOGENOM; CLU_054212_0_0_9; -.
DR   OMA; WGYRNER; -.
DR   OrthoDB; 2029688at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002148; 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: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   PANTHER; PTHR34308; PTHR34308; 1.
DR   Pfam; PF03186; CobD_Cbib; 1.
DR   TIGRFAMs; TIGR00380; cobD; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cobalamin biosynthesis; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..316
FT                   /note="Cobalamin biosynthesis protein CobD"
FT                   /id="PRO_1000057221"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        78..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
SQ   SEQUENCE   316 AA;  35200 MW;  A97A80728C7C5B61 CRC64;
     MTLIAIFLAV LLDWLIGDPY SWPHPVKWMG SYIYLCMRLQ EKKQFSPYLF GFFLWLTTVG
     LALGVSCGLL WLAGLAHPVL YWLVWIYLAY ASLAAKSLAF EAQKVYHTLK FGTLEEARKQ
     VGMIVGRETS QLTPEEISKA TIETVAENTS DGVIGPLLCL FLGGPILAMT YKAINTLDSM
     VGYKTEKYRK IGLISAKMDD LANLIPARLT WLFLILSSQI LLLDVKGALR IGWRDRYQHA
     SPNSAFSEAV VAGALGIQLG GPHVYHGELI EKPTIGEDSR PVEADDIQTA ISLLYTSTMT
     GLILFTLFYL VMQAYF