ID Q1IGP0_PSEE4 Unreviewed; 425 AA.
AC Q1IGP0;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=4-aminobutyrate aminotransferase, PLP-dependent {ECO:0000313|EMBL:CAK13162.1};
DE EC=2.6.1.22 {ECO:0000313|EMBL:CAK13162.1};
GN Name=gabT {ECO:0000313|EMBL:CAK13162.1};
GN OrderedLocusNames=PSEEN0191 {ECO:0000313|EMBL:CAK13162.1};
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK13162.1, ECO:0000313|Proteomes:UP000000658};
RN [1] {ECO:0000313|EMBL:CAK13162.1, ECO:0000313|Proteomes:UP000000658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48 {ECO:0000313|EMBL:CAK13162.1,
RC ECO:0000313|Proteomes:UP000000658};
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CT573326; CAK13162.1; -; Genomic_DNA.
DR RefSeq; WP_011531623.1; NC_008027.1.
DR AlphaFoldDB; Q1IGP0; -.
DR STRING; 384676.PSEEN0191; -.
DR GeneID; 32803541; -.
DR KEGG; pen:PSEEN0191; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000000658; Chromosome.
DR GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00700; GABAtrnsam; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:CAK13162.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:CAK13162.1}.
SQ SEQUENCE 425 AA; 44668 MW; 5ABBE57C77AEE11E CRC64;
MSKTNESLMQ RRVAAVPRGV GQIHPIFVDT AKNSTVIDVE GRELIDFAGG IAVLNTGHLH
PKVVAAVQEQ LTKVSHTCFQ VLAYEPYVEL CEKINARVPG DFAKKTLLVT TGSEAVENAV
KIARAATGRA GVIAFTGGYH GRTMMTLGLT GKVVPYSAGM GLMPGGIFRA LFPSELHGIS
VDDAIASVER IFKNDAEPRD IAAIILEPVQ GEGGFLPAPK ELMKRLRALC DQHGILLIAD
EVQTGAGRTG TFFAMEQMGV APDLTTFAKS IAGGFPLAGV CGKAEYMDAI APGGLGGTYA
GSPIACAAAL AVIEVFEEEK LLERSQAVGE RLTAGLKQIQ AKHPIIGDVR GLGSMIAVEV
FEKGTHTPNA AAVAQVVAKA RDKGLILLSC GTYGNVLRIL VPLTAEDALL DKGLAIIEEC
FAELA
//
