ID E3RNX7_PYRTT Unreviewed; 328 AA. AC E3RNX7; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAR-2024, entry version 46. DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106}; DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106}; DE Flags: Fragment; GN ORFNames=PTT_10298 {ECO:0000313|EMBL:EFQ92582.1}; OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus) OS (Drechslera teres f. teres). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; OC Pyrenophora. OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067}; RN [1] {ECO:0000313|EMBL:EFQ92582.1, ECO:0000313|Proteomes:UP000001067} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ92582.1, RC ECO:0000313|Proteomes:UP000001067}; RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109; RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S., RA Oliver R.P., Friesen T.L.; RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f. RT teres."; RL Genome Biol. 11:R109.1-R109.14(2010). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933}; CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase CC pathway; pyruvate from L-alanine: step 1/1. CC {ECO:0000256|ARBA:ARBA00025708}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. Alanine aminotransferase subfamily. CC {ECO:0000256|ARBA:ARBA00025785}. 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; GL534254; EFQ92582.1; -; Genomic_DNA. DR RefSeq; XP_003299332.1; XM_003299284.1. DR AlphaFoldDB; E3RNX7; -. DR STRING; 861557.E3RNX7; -. DR EnsemblFungi; EFQ92582; EFQ92582; PTT_10298. DR KEGG; pte:PTT_10298; -. DR eggNOG; KOG0258; Eukaryota. DR HOGENOM; CLU_014254_0_0_1; -. DR OrthoDB; 5472891at2759; -. DR UniPathway; UPA00528; UER00586. DR Proteomes; UP000001067; Unassembled WGS sequence. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway. 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; IPR045088; ALAT1/2-like. 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; PTHR11751; ALANINE AMINOTRANSFERASE; 1. DR PANTHER; PTHR11751:SF29; ALANINE TRANSAMINASE; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 3: Inferred from homology; KW Reference proteome {ECO:0000313|Proteomes:UP000001067}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 100..319 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" FT NON_TER 328 FT /evidence="ECO:0000313|EMBL:EFQ92582.1" SQ SEQUENCE 328 AA; 35872 MW; 2FB3B84A89D66C78 CRC64; MSKAPQKVLH IGNINPHVKA AQYAVRGELA VKSEEYRAKL AKGEGKDLPF DTVIAANIGN PQQLDQKPIT FFRQVASILE NPGLLEHEDV LLKSLGYKSD VLERARKLLK EVKSVGAYSQ SQGAPGIRQS VAEYIERRDG FPAKFEDIYL SNGASSGVNT LLHTICAKPE TGIMVPIPQY PLYTATLSVL DARCVPYYLD EEAAWGTSLE SIRTAHEKAV KEGTDVKAIC VINPGNPTGA SLPVEDIKSV LKFAAEKGLV VIADEVYQTN VFIGEFISFK KALRELQKET PGQYDHIELA SLHSVSKGMV GECGHRGGYF ELIGFDPE //