(data stored in SCRATCH zone)

SWISSPROT: B1VNI3_STRGG

ID   B1VNI3_STRGG            Unreviewed;       444 AA.
AC   B1VNI3;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   07-JUN-2017, entry version 60.
DE   SubName: Full=Putative glutamate-1-semialdehyde aminotransferase {ECO:0000313|EMBL:BAG17006.1};
GN   OrderedLocusNames=SGR_177 {ECO:0000313|EMBL:BAG17006.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17006.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17006.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; AP009493; BAG17006.1; -; Genomic_DNA.
DR   RefSeq; WP_012377584.1; NC_010572.1.
DR   ProteinModelPortal; B1VNI3; -.
DR   STRING; 455632.SGR_177; -.
DR   EnsemblBacteria; BAG17006; BAG17006; SGR_177.
DR   GeneID; 6215559; -.
DR   KEGG; sgr:SGR_177; -.
DR   PATRIC; fig|455632.4.peg.155; -.
DR   eggNOG; ENOG4105CDM; Bacteria.
DR   eggNOG; COG0001; LUCA.
DR   HOGENOM; HOG000020210; -.
DR   KO; K01845; -.
DR   OMA; ECGPVTG; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1VNI3.
DR   SWISS-2DPAGE; B1VNI3.
KW   Aminotransferase {ECO:0000313|EMBL:BAG17006.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001685};
KW   Transferase {ECO:0000313|EMBL:BAG17006.1}.
SQ   SEQUENCE   444 AA;  47017 MW;  8C64229712738D2A CRC64;
     MNGFIPALGG TDGSRSWFER AQHSLAGGIS SSSRLTSTGP HPYPLYMASG SGARITDVDG
     NEYIDYLISY GSAVLGHASP LLTEALTQVL HSGTMFGTCN VPEVELAELI CQMVPCAELV
     RFANSGSEAV QGAVRAARGY TGRSAILKFE GHYHGWSDTL AISNRPSAAQ AGPYATPHPV
     PHSPGIPTGV IDDVVVCPWN DPTALRDVLD GHPNLAAVIC EPIVANNACT MPDPDYLDLL
     REECTARDLV LIFDEVCTGF RTGPGGAQNL FGVLPDIAVF SKALGGGLPI AAFAGRRAVM
     EPLARGEVKH GGTYNASPLC ATAALVTLRQ LNDTTVTKRI DEAGQRLMET VRRAAHDNRV
     PCAVQGVGAM FQVVFSSDGA PTRGYRDLLS ADSGRYDAFR HELLKRGVHS NAYAMACWFV
     PAVVSEDDLS ATCQAVEGAF AALR
//

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