ID D2RZ40_HALTV Unreviewed; 439 AA. AC D2RZ40; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAR-2024, entry version 65. DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ADB59964.1}; GN OrderedLocusNames=Htur_1072 {ECO:0000313|EMBL:ADB59964.1}; OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales; OC Natrialbaceae; Haloterrigena. OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB59964.1, ECO:0000313|Proteomes:UP000001903}; RN [1] {ECO:0000313|EMBL:ADB59964.1, ECO:0000313|Proteomes:UP000001903} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 / RC 4k {ECO:0000313|Proteomes:UP000001903}; RX PubMed=21304683; DOI=10.4056/sigs.681272; RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A., RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C., RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N., RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k)."; RL Stand. Genomic Sci. 2:107-116(2010). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933}; CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954, CC ECO:0000256|RuleBase:RU003560}. 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; CP001860; ADB59964.1; -; Genomic_DNA. DR RefSeq; WP_012942273.1; NC_013743.1. DR AlphaFoldDB; D2RZ40; -. DR STRING; 543526.Htur_1072; -. DR GeneID; 8741660; -. DR KEGG; htu:Htur_1072; -. DR eggNOG; arCOG00915; Archaea. DR HOGENOM; CLU_016922_10_0_2; -. DR OrthoDB; 7184at2157; -. DR Proteomes; UP000001903; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR43206:SF2; 4-AMINOBUTYRATE AMINOTRANSFERASE GABT; 1. DR PANTHER; PTHR43206; AMINOTRANSFERASE; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000313|EMBL:ADB59964.1}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, KW ECO:0000256|RuleBase:RU003560}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADB59964.1}. SQ SEQUENCE 439 AA; 48223 MW; 4D3B4F46B9442A87 CRC64; MDRENTVPRV ASFPGSKSKR WVEFHQNTAA PSTYVYDFVW DVTEDATGPF CTDADGNVLM DFTSHVAAAP LGYNHPTLTE QLREFDLVDP MKIAGQDFYV STGGTPEDSS LPGPAHLMDK LTEISSQYDM DTVFLSNSGA EAVENAMKIC YDDCETPKYA ITFDDAFHGR TLGALSLNRS KSVYRRKFPE ISGVHDIEYS QHGLARLRAK LGDSGHIPPE EVGFLILEPI QGEGGYNVPS ASFMSELDDI CSTHDIPIVV DEIQSGVGRT GEMWAVDHFD IEPDVITSAK ALRVGATISR SDLFPDEEAR LSSTWGAGDI LASMQGALTL SVIEEENLLD HATELGTYFR ERLREVAEQT SILTDVRGLG LMIAVEFDTA DHRDEAMETA LRHGLLTLGC GTKTLRLLPP LDVREREIDI CVEIIDDVVD EVADPVPSA //