(data stored in ACNUC7421 zone)
SWISSPROT: Q500F3_PSEU2
ID Q500F3_PSEU2 Unreviewed; 434 AA.
AC Q500F3;
DT 07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2005, sequence version 1.
DT 08-MAY-2019, entry version 79.
DE SubName: Full=4-aminobutyrate aminotransferase apoenzyme {ECO:0000313|EMBL:AAY35219.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:AAY35219.1};
GN OrderedLocusNames=Psyr_0146 {ECO:0000313|EMBL:AAY35219.1};
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35219.1, ECO:0000313|Proteomes:UP000000426};
RN [1] {ECO:0000313|EMBL:AAY35219.1, ECO:0000313|Proteomes:UP000000426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a {ECO:0000313|EMBL:AAY35219.1,
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; AAY35219.1; -; Genomic_DNA.
DR RefSeq; WP_011266223.1; NC_007005.1.
DR RefSeq; YP_233257.1; NC_007005.1.
DR STRING; 205918.Psyr_0146; -.
DR EnsemblBacteria; AAY35219; AAY35219; Psyr_0146.
DR GeneID; 3365622; -.
DR KEGG; psb:Psyr_0146; -.
DR PATRIC; fig|205918.7.peg.143; -.
DR eggNOG; ENOG4108JPW; Bacteria.
DR eggNOG; COG0160; LUCA.
DR HOGENOM; HOG000020206; -.
DR KO; K07250; -.
DR OMA; TGMSQPY; -.
DR BioCyc; PSYR205918:G1G4J-147-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; Q500F3.
DR SWISS-2DPAGE; Q500F3.
KW Aminotransferase {ECO:0000313|EMBL:AAY35219.1};
KW Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW Transferase {ECO:0000313|EMBL:AAY35219.1}.
SQ SEQUENCE 434 AA; 46625 MW; 88909DB1285664BF CRC64;
MNSKVDETPH LLRQRDQFVP RGIVTAHPLV IDRAQGSELW DVDGKRYLDF VGGIGVLNIG
HNHPNVVKAI QAQLTKVTHA CFQVASYQPY LDLAKRLSHL IAGQSGIDHK AVLFTSGAEA
VENAVKIARA HTNRPAIISF RGGFHGRTLL GTTLTGMSQP YKQNFGPMAP EVFHTPYPNE
YRGVTTDVAL AALHELLATQ VAPERVAAIL IEPMQGDGGF LTAPVEFMKA LRALTEQHGI
VLIADEIQSG FGRTGKWFGF EHSGIQPDLV TVAKSLAGGM PLSGVVGRAE IMDAPLPGGL
GGTYGGNALS CAAALAVIDT YEQENLLARG EQLGNQLRAG LLKLKERYSC IGDVRGTGFM
LAMEMVKNDA ARSPDADLNQ KVIDQARLGG LLVIKCGVYR NVLRFLAPLV TTEQQIDEAL
GILDAALARV LKSS
//
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