ID A0A498H1N8_9EURY Unreviewed; 376 AA. AC A0A498H1N8; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 02-DEC-2020, entry version 10. DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481}; DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481}; GN ORFNames=ABH15_01510 {ECO:0000313|EMBL:RXE56859.1}; OS Methanoculleus taiwanensis. OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus. OX NCBI_TaxID=1550565 {ECO:0000313|EMBL:RXE56859.1, ECO:0000313|Proteomes:UP000290932}; RN [1] {ECO:0000313|EMBL:RXE56859.1, ECO:0000313|Proteomes:UP000290932} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CYW4 {ECO:0000313|EMBL:RXE56859.1, RC ECO:0000313|Proteomes:UP000290932}; RX PubMed=25575827; DOI=.1099/ijs.0.000062; RA Weng C.Y., Chen S.C., Lai M.C., Wu S.Y., Lin S., Yang T.F., Chen P.C.; RT "Methanoculleus taiwanensis sp. nov., a methanogen isolated from deep RT marine sediment at the deformation front area near Taiwan."; RL Int. J. Syst. Evol. Microbiol. 65:1044-1049(2015). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RXE56859.1}. 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; LHQS01000001; RXE56859.1; -; Genomic_DNA. DR Proteomes; UP000290932; Unassembled WGS sequence. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW. 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; IPR015422; PyrdxlP-dep_Trfase_dom1. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605}; KW Aminotransferase {ECO:0000256|RuleBase:RU000481, KW ECO:0000313|EMBL:RXE56859.1}; KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102}; KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:RXE56859.1}. FT DOMAIN 32..373 FT /note="Aminotran_1_2" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 376 AA; 41029 MW; 79FC2BC1774052F7 CRC64; MRRLSEKVAG IAPSATIEIS NAAKRMVQEG IDVISLSIGE PDFDTPKHIT DACIDALRRG ETHYAPSQGI PELTAAIAEK ITSENGFSAS PDQVIVTCGA KDAIYEAMEA VVNPGDEVLI LDPAWVSYEP CVQLAGGTTR HHAVDQETFQ LDDSLLEAVN GNTRMIVVNS PSNPSGAVLD ERSLQLVADI CTDHDIVALS DEIYEKLVYD KEHISLAGLG DMAERTITIN GFSKAYAMTG WRIGYAVAPE RIIRQMNKVQ QHTISHPATF AMFGAVAALT GDQCCVEEMR REFLQRRDYV IAALHGMGYR TAPADGAFYA YVKVEGDDME IARRWLREAH VAVTPGSAFG TPGWERLSYA TSTANLKEAM YRISTV //