(data stored in SCRATCH zone)

SWISSPROT: Q500K8_PSEU2

ID   Q500K8_PSEU2            Unreviewed;       426 AA.
AC   Q500K8;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   SubName: Full=4-aminobutyrate aminotransferase apoenzyme {ECO:0000313|EMBL:AAY35164.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:AAY35164.1};
GN   OrderedLocusNames=Psyr_0090 {ECO:0000313|EMBL:AAY35164.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35164.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35164.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35164.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000075; AAY35164.1; -; Genomic_DNA.
DR   RefSeq; WP_003401617.1; NC_007005.1.
DR   RefSeq; YP_233202.1; NC_007005.1.
DR   STRING; 205918.Psyr_0090; -.
DR   EnsemblBacteria; AAY35164; AAY35164; Psyr_0090.
DR   GeneID; 3365565; -.
DR   KEGG; psb:Psyr_0090; -.
DR   PATRIC; fig|205918.7.peg.90; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K14268; -.
DR   OMA; VNNVGHC; -.
DR   BioCyc; PSYR205918:G1G4J-90-MONOMER; -.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00700; GABAtrnsam; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q500K8.
DR   SWISS-2DPAGE; Q500K8.
KW   Aminotransferase {ECO:0000313|EMBL:AAY35164.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:AAY35164.1}.
SQ   SEQUENCE   426 AA;  44989 MW;  E39A64212A49A37B CRC64;
     MSKTNESLMQ RRHAAVPRGV GQIHPIFAAS AKNATVTDVE GREFIDFAGG IAVLNTGHLH
     PKIIAAVQEQ LTKLSHTCFQ VLAYEPYVEL CEKINAKVPG DFDKKTLLVT TGSEAVENAV
     KIARAATGRA GVIAFTGAYH GRTMMTLGLT GKVVPYSAGM GLMPGGIFRA LYPCELHGVS
     VDDSIASIER IFKNDAEPKD IAAIIIEPVQ GEGGFYVAPK AFMLRLRELC DKHGILLIAD
     EVQTGAGRTG TFFAMEQMGV AADLTTFAKS IAGGFPLAGV CGKAEYMDAI APGGLGGTYA
     GSPVACAAAL AVLDIFEEEH LLERCKAVGE QLVTSLKAMQ AKYPVIGEVR ALGAMIAVEL
     FEDGDSHKPN AAAVAQVVAK ARDKGLILLS CGTYGNVLRV LVPLTAEDEL LKRGLAILDE
     CFAEIA
//

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