ID Q48RP8_STRPM Unreviewed; 404 AA. AC Q48RP8; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 2. DT 24-JAN-2024, entry version 95. DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106}; DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106}; GN OrderedLocusNames=M28_Spy1502 {ECO:0000313|EMBL:AAX72612.2}; OS Streptococcus pyogenes serotype M28 (strain MGAS6180). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=319701 {ECO:0000313|EMBL:AAX72612.2, ECO:0000313|Proteomes:UP000009292}; RN [1] {ECO:0000313|EMBL:AAX72612.2, ECO:0000313|Proteomes:UP000009292} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGAS6180 {ECO:0000313|EMBL:AAX72612.2, RC ECO:0000313|Proteomes:UP000009292}; RX PubMed=16088825; DOI=10.1086/430618; RA Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D., Beres S.B., RA LeFebvre R.B., Musser J.M.; RT "Genome sequence of a serotype M28 strain of group A Streptococcus: RT potential new insights into puerperal sepsis and bacterial disease RT specificity."; RL J. Infect. Dis. 192:760-770(2005). 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; CP000056; AAX72612.2; -; Genomic_DNA. DR RefSeq; WP_010922605.1; NC_007296.2. DR AlphaFoldDB; Q48RP8; -. DR KEGG; spb:M28_Spy1502; -. DR HOGENOM; CLU_017584_4_2_9; -. DR Proteomes; UP000009292; 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:AAX72612.2}; KW Transferase {ECO:0000313|EMBL:AAX72612.2}. FT DOMAIN 34..394 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 404 AA; 45223 MW; 30D9D2499183A217 CRC64; MKIIEKSSKL EHVAYDIRGP VLDEANRMIA SGEKILRLNT GNPAAFGFEA PDEVIRDLIV NARLSEGYSD SKGIFSARKA IMQYCQLKGF PDVDIEDIYL GNGVSELISI SLQALLDNGD EVLVPMPDYP LWTACVSLGG GKAVHYLCDE EAGWYPDIAD IKSKITSRTK AIVVINPNNP TGALYPKEIL EDIVALAREH QLIIFADEIY DRLVMDGKEH IAIASLAPDV FCVSMNGLSK SHRIAGFRVG WMVLSGPKDH VKGYIEGLNM LANMRLCSNV LAQQVVQTSL GGHQSVDALL LPGGRIFEQR NFIYEAINAI PGLSAVKPEA GLYLFPKIDR QMYRIDDDEE FVLQLLKQEK VMLVHGRGFN WKDPDHFRIV YLPSVEELED VQEKITRVLY QYRR //