ID K0F8I8_NOCB7 Unreviewed; 418 AA. AC K0F8I8; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 24-JAN-2024, entry version 38. DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106}; DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106}; GN ORFNames=O3I_040410 {ECO:0000313|EMBL:AFU06027.1}; OS Nocardia brasiliensis (strain ATCC 700358 / HUJEG-1). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae; OC Nocardia. OX NCBI_TaxID=1133849 {ECO:0000313|EMBL:AFU06027.1, ECO:0000313|Proteomes:UP000006304}; RN [1] {ECO:0000313|EMBL:AFU06027.1, ECO:0000313|Proteomes:UP000006304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700358 {ECO:0000313|Proteomes:UP000006304}; RX PubMed=22535940; DOI=10.1128/JB.00210-12; RA Vera-Cabrera L., Ortiz-Lopez R., Elizondo-Gonzalez R., Perez-Maya A.A., RA Ocampo-Candiani J.; RT "Complete genome sequence of Nocardia brasiliensis HUJEG-1."; RL J. Bacteriol. 194:2761-2762(2012). 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; CP003876; AFU06027.1; -; Genomic_DNA. DR RefSeq; WP_014988874.1; NC_018681.1. DR AlphaFoldDB; K0F8I8; -. DR STRING; 1133849.O3I_040410; -. DR GeneID; 80365665; -. DR KEGG; nbr:O3I_040410; -. DR eggNOG; COG0436; Bacteria. DR HOGENOM; CLU_017584_4_2_11; -. DR Proteomes; UP000006304; Chromosome. DR GO; GO:0004021; F:L-alanine: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:AFU06027.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006304}; KW Transferase {ECO:0000313|EMBL:AFU06027.1}. FT DOMAIN 48..395 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 418 AA; 46051 MW; 7990B12357F84CE5 CRC64; MGRVSPSHLP HRPPRVLEQS TKLQNVVYEI RGPVHAQAAR LEAEGHRILK LNIGNPAPFG FEAPDVIMRD IIASLPYAQG YSESKGITSA RRAVVTRYEL VPGFPELDVD DVYLGNGVSE LITITMQALL DNGDEVLIPA PDYPLWTAMT SLAGGTPVHY LCDESSGWQP DIADIESKIT DKTKALLVIN PNNPTGAVYS AEILQQLADI ARKHQLLLLA DEIYDKILYD DAKHVSMASV APDLLCLTFN GLSKAYRVAG YRSGWLAITG PKEHAAGFLE GIDLLASSRL CPNVPAQHAI QVALGGHQSI EDLILPGGRL LEQRDVAWER LNMIPGVSCV KPKGALYAFP RLDPNVYEIH DDSKLILDLL LQEKILMVQG TGFNWPNHDH LRIVTLPWAR DLAVAIERFG NFLSSYRQ //