ID Q24Y81_DESHY Unreviewed; 398 AA. AC Q24Y81; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 07-SEP-2016, entry version 65. DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481}; DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481}; GN OrderedLocusNames=DSY1222 {ECO:0000313|EMBL:BAE83011.1}; OS Desulfitobacterium hafniense (strain Y51). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitobacterium. OX NCBI_TaxID=138119 {ECO:0000313|Proteomes:UP000001946}; RN [1] {ECO:0000313|EMBL:BAE83011.1, ECO:0000313|Proteomes:UP000001946} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y51 {ECO:0000313|Proteomes:UP000001946}; RX PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006; RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K., RA Inatomi K., Furukawa K., Inui M., Yukawa H.; RT "Complete genome sequence of the dehalorespiring bacterium RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides RT ethenogenes 195."; RL J. Bacteriol. 188:2262-2274(2006). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU000481}; CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|RuleBase:RU000481}. 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; AP008230; BAE83011.1; -; Genomic_DNA. DR RefSeq; WP_011459580.1; NC_007907.1. DR ProteinModelPortal; Q24Y81; -. DR STRING; 138119.DSY1222; -. DR EnsemblBacteria; BAE83011; BAE83011; DSY1222. DR KEGG; dsy:DSY1222; -. DR PATRIC; 21670788; VBIDesHaf65307_1361. DR eggNOG; ENOG4105CHM; Bacteria. DR eggNOG; COG0436; LUCA. DR HOGENOM; HOG000223055; -. DR KO; K11358; -. DR OMA; AYKENRD; -. DR OrthoDB; POG091H011K; -. DR BioCyc; DHAF138119:GHT5-1249-MONOMER; -. DR Proteomes; UP000001946; 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 Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000256|RuleBase:RU000481}; KW Complete proteome {ECO:0000313|Proteomes:UP000001946}; KW Reference proteome {ECO:0000313|Proteomes:UP000001946}; KW Transferase {ECO:0000256|RuleBase:RU000481}. FT DOMAIN 35 383 Aminotran_1_2. {ECO:0000259|Pfam: FT PF00155}. SQ SEQUENCE 398 AA; 44220 MW; F5ACEAE48E1F9C08 CRC64; MISRTMQQQV NSSSIIRAMF EEGKRLSALY GADNVYDFSL GNPNVEPPAE VKQAIMDILN EENSTTVHGY MNNSGFEDVR GAIAASLNQR FATGFAADNI LMTVGAAGGL NVIFKTLLNP EDEVLTFAPF FGEYRNYVQN YQGQLIVVSP NTKDFQPNLE ELKEKISPRT KAVLINSPNN PTGVVYSAET IAALVDILRA KQEEYGTVIY LIGDEPYREL AYDQVEVPYL TKYYENTIVG YSYSKSLSLP GERIGYLVIP REAADYENLI AAANIANRIL GFVNAPSLFQ RVIAKCLDAQ VNLDSYNRNR ELLYNALVSY GYQCIKPEGA FYLFIKTPLE NDLEFCTLAK SKNILIVPGT SFACPGYARI AYCVAYETIE RALPGFEALI NEVSWASA //