ID D4HX11_ERWAC Unreviewed; 405 AA. AC D4HX11; DT 18-MAY-2010, integrated into UniProtKB/TrEMBL. DT 18-MAY-2010, sequence version 1. DT 27-MAR-2024, entry version 59. DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106}; DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106}; GN Name=aat3 {ECO:0000313|EMBL:CBA21607.1}; GN OrderedLocusNames=EAMY_2376 {ECO:0000313|EMBL:CBA21607.1}; OS Erwinia amylovora (strain CFBP1430). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Erwinia. OX NCBI_TaxID=665029 {ECO:0000313|EMBL:CBA21607.1, ECO:0000313|Proteomes:UP000001841}; RN [1] {ECO:0000313|EMBL:CBA21607.1, ECO:0000313|Proteomes:UP000001841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFBP1430 {ECO:0000313|Proteomes:UP000001841}; RX PubMed=20192826; DOI=10.1094/MPMI-23-4-0384; RA Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E., RA Duffy B.; RT "Complete genome sequence of the fire blight pathogen Erwinia amylovora RT CFBP 1430 and comparison to other Erwinia spp."; RL Mol. Plant Microbe Interact. 23:384-393(2010). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933}; CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}. 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; FN434113; CBA21607.1; -; Genomic_DNA. DR RefSeq; WP_004158618.1; NC_013961.1. DR AlphaFoldDB; D4HX11; -. DR STRING; 665029.EAMY_2376; -. DR GeneID; 8913259; -. DR KEGG; eam:EAMY_2376; -. DR PATRIC; fig|665029.3.peg.2290; -. DR eggNOG; COG0436; Bacteria. DR HOGENOM; CLU_017584_4_2_6; -. DR OrthoDB; 9803354at2; -. DR Proteomes; UP000001841; Chromosome. DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1. DR PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000313|EMBL:CBA21607.1}; KW Transferase {ECO:0000313|EMBL:CBA21607.1}. FT DOMAIN 34..388 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 405 AA; 45257 MW; A09D8B2125739374 CRC64; MTPIEKSGKL DNVCYDIRGP VLKEARRLEE EGNKVLKLNI GNPAPFGFEA PDEILVDVIR NLPGAQGYCD SKGLYSARKA IMQHYQAHGM RDVTVEDIYI GNGVSELIVQ SMQALLNSGD EMLVPAPDYP LWTAAVSLSG GKAVHYMCDE SAGWFPDLDD IRSKITPRTR GIVIINPNNP TGAVYSKELL SEVVELARQH NLIIFADEIY DKILYDAAQH HSIAALAPDL LTITFNGLSK TYRVAGFRQG WMVLNGPKKH AKGYIEGLEM LASMRLCANV PAQHAIQTAL GGYQSISEFI QPGGRLYEQR NRAWELINEI PGVSCVKPDG ALYMFPKINS KKFNIHDDQK MVLDFLLQEK VLLVQGSAFN WPWPDHVRIV TLPRVDELEM AIGKFDRFLS GYRQL //