(data stored in SCRATCH zone)

SWISSPROT: A5GRI7_SYNR3

ID   A5GRI7_SYNR3            Unreviewed;       311 AA.
AC   A5GRI7;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   16-JAN-2019, entry version 65.
DE   RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN   Name=cbiB {ECO:0000313|EMBL:CAK27496.1};
GN   Synonyms=cobD {ECO:0000256|HAMAP-Rule:MF_00024,
GN   ECO:0000313|EMBL:CAK27496.1};
GN   OrderedLocusNames=SynRCC307_0593 {ECO:0000313|EMBL:CAK27496.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27496.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-Rule:MF_00024}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00024}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00024}.
CC   -!- SIMILARITY: Belongs to the CobD/CbiB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00024}.
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DR   EMBL; CT978603; CAK27496.1; -; Genomic_DNA.
DR   RefSeq; WP_011935011.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0593; -.
DR   EnsemblBacteria; CAK27496; CAK27496; SynRCC307_0593.
DR   KEGG; syr:SynRCC307_0593; -.
DR   eggNOG; ENOG4105DH2; Bacteria.
DR   eggNOG; COG1270; LUCA.
DR   HOGENOM; HOG000290070; -.
DR   KO; K02227; -.
DR   OMA; DAMVGHR; -.
DR   OrthoDB; 2029688at2; -.
DR   BioCyc; SSP316278:G1GJL-579-MONOMER; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001115; 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:cobalamin-transporting ATPase activity; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR34308; PTHR34308; 1.
DR   Pfam; PF03186; CobD_Cbib; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GRI7.
DR   SWISS-2DPAGE; A5GRI7.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00024};
KW   Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00024};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Ligase {ECO:0000313|EMBL:CAK27496.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00024};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00024}.
SQ   SEQUENCE   311 AA;  32559 MW;  C9B61D2AEBDF40E0 CRC64;
     MAAACGLDRL IGDPRWCLHP VQVMGAVIAQ LRLWVEALGG DRPWALRLGG GLITALLVSG
     SAAAGWALEQ LSLRSPWAMP LLVIALASAL AGRSLRLAVE DVIKPLSSAP PQLQQARQKL
     AWIVGRDVDG LPAPELLRAL AETASENAVD GLFAPLFWML IGAGLWGLNP ALPGPLALAW
     AFKASSTLDS MLGYRRGRLQ WLGTAGARLD DGLTWLPCRL LALSLGQLGP ALRDGASDPS
     PNAGVSQAAY AHALGLRLGG LNRYGGIERA KPLLNEGGRA ADEKGVQAIL DVSQRSALLW
     LGLSGVVALL A
//

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