ID D4GHQ4_PANAM Unreviewed; 438 AA. AC D4GHQ4; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAR-2024, entry version 62. DE SubName: Full=GabT {ECO:0000313|EMBL:ADD77571.1}; GN Name=gabT {ECO:0000313|EMBL:ADD77571.1}; GN OrderedLocusNames=PANA_2404 {ECO:0000313|EMBL:ADD77571.1}; OS Pantoea ananatis (strain LMG 20103). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Pantoea. OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD77571.1, ECO:0000313|Proteomes:UP000001702}; RN [1] {ECO:0000313|EMBL:ADD77571.1, ECO:0000313|Proteomes:UP000001702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD77571.1, RC ECO:0000313|Proteomes:UP000001702}; RX PubMed=20348253; DOI=10.1128/JB.00060-10; RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F., RA Coutinho T.A.; RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of RT Eucalyptus blight and dieback."; RL J. Bacteriol. 192:2936-2937(2010). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001875; ADD77571.1; -; Genomic_DNA. DR RefSeq; WP_013026283.1; NC_013956.2. DR AlphaFoldDB; D4GHQ4; -. DR STRING; 706191.PANA_2404; -. DR GeneID; 57267698; -. DR KEGG; pam:PANA_2404; -. DR eggNOG; COG0160; Bacteria. DR HOGENOM; CLU_016922_10_0_6; -. DR Proteomes; UP000001702; Chromosome. 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; 2. 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, KW ECO:0000256|RuleBase:RU003560}; KW Reference proteome {ECO:0000313|Proteomes:UP000001702}; KW Transferase {ECO:0000256|ARBA:ARBA00022576}. SQ SEQUENCE 438 AA; 47039 MW; 444AFA670665BA98 CRC64; MQNVLAEQQT YADNSQLLDV RDHNVPRGII TAHPLVIERA KGSEVWDVEG NRYLDFVGGI GVLNVGHNHP AVVNAVTRQL GMVSHACFQV AAYPGYIELA QRLNKLVGGD EHYKSVFFTS GAEAVENAVK IARSYTQRPG IIAFDGAFHG RTLLGVTLTG MSAPYKQNFG PFPGDVYRLP FPNPLHGVTE ADCLKALDQL FSVQILPERV AAIIIEPVQG DGGFLPAGPA FMQALRRITT QHGIMLICDE IQSGFGRTGT MFAFQQLGIK PDMITTAKSL AGGLPISGVV GKAEIMDSPA PGGLGGTYGG NALACAAALA VLDIFEQENL LARSCQLGEQ LNQRLRQLAD KYACIGDVRG VGFMQAVEIL DVDTHKPDSA LTQKILDSAC QEGLLLIKCG LHRNTIRFLA PLVTTDSQLE EALHIFDIAL ARATGRLG //