(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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