ID F8A8C4_THEID Unreviewed; 407 AA. AC F8A8C4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAR-2024, entry version 54. DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481}; DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481}; GN OrderedLocusNames=Thein_0043 {ECO:0000313|EMBL:AEH43928.1}; OS Thermodesulfatator indicus (strain DSM 15286 / JCM 11887 / CIR29812). OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria; OC Thermodesulfobacteriales; Thermodesulfatatoraceae; Thermodesulfatator. OX NCBI_TaxID=667014 {ECO:0000313|EMBL:AEH43928.1, ECO:0000313|Proteomes:UP000006793}; RN [1] {ECO:0000313|Proteomes:UP000006793} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15286 / JCM 11887 / CIR29812 RC {ECO:0000313|Proteomes:UP000006793}; RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders L., RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Thermodesulfatator indicus DSM 15286."; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEH43928.1, ECO:0000313|Proteomes:UP000006793} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15286 / JCM 11887 / CIR29812 RC {ECO:0000313|Proteomes:UP000006793}; RX PubMed=22768359; DOI=10.4056/sigs.2665915; RA Anderson I., Saunders E., Lapidus A., Nolan M., Lucas S., Tice H., RA Del Rio T.G., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S., RA Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Chang Y.J., RA Brambilla E.M., Rohde M., Spring S., Goker M., Detter J.C., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of the thermophilic sulfate-reducing ocean RT bacterium Thermodesulfatator indicus type strain (CIR29812(T))."; RL Stand. Genomic Sci. 6:155-164(2012). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|RuleBase:RU000481}; CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441, CC 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; CP002683; AEH43928.1; -; Genomic_DNA. DR RefSeq; WP_013906675.1; NC_015681.1. DR AlphaFoldDB; F8A8C4; -. DR STRING; 667014.Thein_0043; -. DR PaxDb; 667014-Thein_0043; -. DR KEGG; tid:Thein_0043; -. DR PATRIC; fig|667014.3.peg.47; -. DR eggNOG; COG0436; Bacteria. DR HOGENOM; CLU_017584_4_2_0; -. DR InParanoid; F8A8C4; -. DR OrthoDB; 9804474at2; -. DR Proteomes; UP000006793; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0006520; P:amino acid metabolic process; 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; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR InterPro; IPR005958; TyrNic_aminoTrfase. DR NCBIfam; TIGR01265; tyr_nico_aTase; 1. 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 PIRSF; PIRSF000517; Tyr_transaminase; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000256|RuleBase:RU000481, KW ECO:0000313|EMBL:AEH43928.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006793}; KW Transferase {ECO:0000256|RuleBase:RU000481}. FT DOMAIN 37..389 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 407 AA; 45418 MW; 0A38C813D64FD001 CRC64; MKRDFEPIKP AKRTENIEYA VRDIVLVANE ARKKGKELIF LNIGDPAQFD FRTPEPIIEA TYQAMCENLT GYSASEGVDE AICAIRKEAR KAGIEPSDIY VTSGASEAID FALTALVNEG ENVLVPYPGY PLYTAILAKL GAEPNPYYLD EENEWQPDLA DIEAKINEKT RAIVIINPNN PTGAVYSEET LRGIIDIARR HQLVIFSDEI YDKLVFDGAK HISIASLDLE VPVVTFNGLS KSYLAPGFRI GWGIVSGPWE VVKDFVEAIH KLARARLSAS HPKQYAIPVA LNGNQGHLKE VIEKLEKRRD LTYEMLNDIP GISCVKPKGA FYAFPRIDIP EVSDREFVKE LIAETGVVVV HGSGFGEKPG TAHFRVVFLP PEDLLKKAYT RIKDFMKKFL ARRGLRA //