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Database: UniProt/TrEMBL
Entry: A5VM86_LACRD
LinkDB: A5VM86_LACRD
Original site: A5VM86_LACRD 
ID   A5VM86_LACRD            Unreviewed;       319 AA.
AC   A5VM86;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   01-MAY-2013, entry version 42.
DE   RecName: Full=Cobalamin biosynthesis protein CobD;
GN   Name=cobD; OrderedLocusNames=Lreu_1721;
OS   Lactobacillus reuteri (strain DSM 20016).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=557436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20016;
RX   PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA   Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA   Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA   Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L.,
RA   Ivanova N., Kyrpides N.C., Walter J.;
RT   "The evolution of host specialization in the vertebrate gut symbiont
RT   Lactobacillus reuteri.";
RL   PLoS Genet. 7:E1001314-E1001314(2011).
CC   -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC       aminopropanol on the F carboxylic group (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the CobD/CbiB family.
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DR   EMBL; CP000705; ABQ83960.1; -; Genomic_DNA.
DR   RefSeq; YP_001272297.1; NC_009513.1.
DR   STRING; 557436.Lreu_1721; -.
DR   EnsemblBacteria; ABQ83960; ABQ83960; Lreu_1721.
DR   GeneID; 5188933; -.
DR   KEGG; lre:Lreu_1721; -.
DR   PATRIC; 22256703; VBILacReu87937_1739.
DR   eggNOG; COG1270; -.
DR   HOGENOM; HOG000290070; -.
DR   KO; K02227; -.
DR   OMA; REFGWAS; -.
DR   ProtClustDB; CLSK2326635; -.
DR   UniPathway; UPA00148; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015420; F:cobalamin-transporting ATPase activity; IEA:HAMAP.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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   Pfam; PF03186; CobD_Cbib; 1.
DR   TIGRFAMs; TIGR00380; cobD; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cobalamin biosynthesis; Complete proteome; Ligase;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   TRANSMEM     53     73       Helical; (By similarity).
FT   TRANSMEM     76     96       Helical; (By similarity).
FT   TRANSMEM    154    174       Helical; (By similarity).
FT   TRANSMEM    204    224       Helical; (By similarity).
FT   TRANSMEM    298    318       Helical; (By similarity).
SQ   SEQUENCE   319 AA;  36044 MW;  24904A9F686BE7B3 CRC64;
     MNILIMVILA FIFDFLLGDP HSWPHPVKAM GHLIAYLTKK FNRSNYSTKR KKWFGALTWL
     ITVGGSGLIT YILMRFAAIN YYLYMIVGTY LCYTCLSMRQ LAIEAEKIMK SLQQNNLNKA
     RQQVGMIVGR DTNQLSAEEV TKATIETVAE NTSDGVIAPL FFLVIGGPVL GIMYKAINTL
     DSMIGYQNEK FRAFGEVSAR IDDIANYVPA RITWLLLIIS SWLLRDDTRE AIAVGERDCE
     KHLSPNSAFS EAVVAGALHL QLGGPHYYFG ELVKKPYIGN DHLVIAANWH LKRTITMLYL
     TSFLGLCGFE LIRFLIVWK
//
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