ID E1T6R4_BURSG Unreviewed; 422 AA. AC E1T6R4; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAR-2024, entry version 49. DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106}; DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106}; GN OrderedLocusNames=BC1003_1519 {ECO:0000313|EMBL:ADN57490.1}; OS Burkholderia sp. (strain CCGE1003). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN57490.1}; RN [1] {ECO:0000313|EMBL:ADN57490.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN57490.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., RA Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.; RT "Complete sequence of chromosome1 of Burkholderia sp. CCGE1003."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. 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; CP002217; ADN57490.1; -; Genomic_DNA. DR AlphaFoldDB; E1T6R4; -. DR STRING; 640512.BC1003_1519; -. DR KEGG; bgf:BC1003_1519; -. DR eggNOG; COG0436; Bacteria. DR HOGENOM; CLU_017584_4_2_4; -. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. 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:ADN57490.1}; KW Transferase {ECO:0000313|EMBL:ADN57490.1}. FT DOMAIN 45..401 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 422 AA; 46916 MW; C29872E352676553 CRC64; MPINQDEVPA VKPILKSNKL LNVCYDIRGP VLEHAKRLEE EGHRIIKLNI GNLAPFGFEA PDEIIQDMIL NLPGSSGYSD SKGVFAARKA IMHYTQQKGV HGVELDDIYI GNGASELIVM ALQGLLNDGD EVLLPAPDYP LWTAGVSLAG GTPVHYICDE SNRWMPDLDD IRAKITPNTR ALVVINPNNP TGALYSDELL LGLIEIARQH GLVIFADEVY DKIVYDGKKH TSMAALSEDV LTVTFNSLSK SYRSCGYRAG WMFISGLTGE NRRHAKDYFE GLGILASMRL CPNVPGQYAI QTALGGYQSI NDLIVPGGRL YKQRELAYDM LTAIPGVSCV KPEAALYMFP RLDPKVYPIQ NDQQFILDLL LEERVLLVQG TGFNWKTPDH FRVVFLPNVD DLADSINRIA RFLDGYRKRH TA //