ID Q0HVD1_SHESR Unreviewed; 404 AA. AC Q0HVD1; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 80. DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106}; DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106}; GN OrderedLocusNames=Shewmr7_1935 {ECO:0000313|EMBL:ABI42924.1}; OS Shewanella sp. (strain MR-7). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=60481 {ECO:0000313|EMBL:ABI42924.1}; RN [1] {ECO:0000313|EMBL:ABI42924.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MR-7 {ECO:0000313|EMBL:ABI42924.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K., RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.; RT "Complete sequence of Chromosome1 of Shewanella sp. MR-7."; RL Submitted (AUG-2006) 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; CP000444; ABI42924.1; -; Genomic_DNA. DR AlphaFoldDB; Q0HVD1; -. DR KEGG; shm:Shewmr7_1935; -. DR HOGENOM; CLU_017584_4_2_6; -. 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:ABI42924.1}; KW Transferase {ECO:0000313|EMBL:ABI42924.1}. FT DOMAIN 35..392 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 404 AA; 45391 MW; 3C36600121E6B570 CRC64; MRPIIKSNKL DTVCYDIRGP VHKEARRLED EGHRILKLNI GNPAPFGFEA PEEIVRDVIL NLPSAQGYCE SKGLFSARKA IVQHYQAQGI FGVDIEDIYI GNGVSELIMM AMQGLLNTDD EILIPSPDYP LWTAAANLAG GKAVHYRCDE DADWFPDLDD IKSKISSRTR GIVLINPNNP TGAVYSKELL LQVVELCREH NLILFADEIY DKILYDEAKH IPAASLSDDI LTVTFNGLSK AYRAAGFRVG WMMLSGNLKA AKSYIEGLEM LSSMRLCANV PNQHAIQTAL GGYQSINELI LPSGRLTVQR DTCYELLNQI PGVSVKKPKG ALYAFPKLDM KKFNLRDDER LVLDLLREKK ILLVHGSAFN WPEPDHLRVV FLPYKEDLTK ALTEFGHFLE TYKQ //