ID G2NAR9_STREK Unreviewed; 403 AA. AC G2NAR9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 53. DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106}; DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106}; GN ORFNames=SACTE_1402 {ECO:0000313|EMBL:AEN09320.1}; OS Streptomyces sp. (strain SirexAA-E / ActE). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN09320.1, ECO:0000313|Proteomes:UP000001397}; RN [1] {ECO:0000313|EMBL:AEN09320.1, ECO:0000313|Proteomes:UP000001397} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K., RA Adams S., Book A., Currie C., Woyke T.; RT "Complete sequence of Streptomyces sp. SirexAA-E."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEN09320.1, ECO:0000313|Proteomes:UP000001397} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397}; RX PubMed=24710170; DOI=10.1371/journal.pone.0094166; RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F., RA Book A.J., Currie C.R., Fox B.G.; RT "Biochemical properties and atomic resolution structure of a RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp. RT SirexAA-E."; RL PLoS ONE 9:e94166-E94166(2014). 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; CP002993; AEN09320.1; -; Genomic_DNA. DR RefSeq; WP_014045308.1; NC_015953.1. DR AlphaFoldDB; G2NAR9; -. DR STRING; 862751.SACTE_1402; -. DR KEGG; ssx:SACTE_1402; -. DR PATRIC; fig|862751.12.peg.1462; -. DR eggNOG; COG0436; Bacteria. DR HOGENOM; CLU_017584_4_2_11; -. DR OrthoDB; 9763453at2; -. DR Proteomes; UP000001397; Chromosome. 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:AEN09320.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001397}; KW Transferase {ECO:0000313|EMBL:AEN09320.1}. FT DOMAIN 34..394 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 403 AA; 44689 MW; CA14F6C302A64A06 CRC64; MEFRQSSKLN EVCYEIRGPV IEQANALEEA GHSVLRLNTG NPALFGFEAP EEIVQDMIRM LPQAHGYTDS RGILSARRAV AQRYQAMGLA DVDVDDVFLG NGVSELISMA VQALLEDGDE VLIPSPDYPL WTAVTTLAGG KAVHYTCDES ADWNPDLADM ASKITDRTRA VVIINPNNPT GAVYPREVLD GILDLARRHG LMVFADEIYD QILYDDAEHH PVSVLAPDLL CLTFSGLSKT YRVAGFRSGW MVVSGPQQHA RNYLEGLTTL ASMRLCPNAP AQYAIQAALG GRQSIRELVA PGGRLHEQRD RAWERLNEIP GVSCVKPKGA LYAFPRIDPK VHAIVDDERF VLDLLLREKI QVVQGTGFNW PRPDHFRILT LPYADDLDAA ISRIGRFLNG YRQ //