ID C5A369_THEGJ Unreviewed; 445 AA.
AC C5A369;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Pyridoxal phosphate-dependent aminotransferase, class III family {ECO:0000313|EMBL:ACS32681.1};
GN OrderedLocusNames=TGAM_0179 {ECO:0000313|EMBL:ACS32681.1};
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117 {ECO:0000313|EMBL:ACS32681.1, ECO:0000313|Proteomes:UP000001488};
RN [1] {ECO:0000313|EMBL:ACS32681.1, ECO:0000313|Proteomes:UP000001488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3
RC {ECO:0000313|Proteomes:UP000001488};
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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|RuleBase:RU003560}.
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DR EMBL; CP001398; ACS32681.1; -; Genomic_DNA.
DR RefSeq; WP_015857801.1; NC_012804.1.
DR AlphaFoldDB; C5A369; -.
DR STRING; 593117.TGAM_0179; -.
DR PaxDb; 593117-TGAM_0179; -.
DR GeneID; 7988759; -.
DR KEGG; tga:TGAM_0179; -.
DR PATRIC; fig|593117.10.peg.181; -.
DR eggNOG; arCOG00915; Archaea.
DR HOGENOM; CLU_016922_10_0_2; -.
DR OrthoDB; 6534at2157; -.
DR Proteomes; UP000001488; 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; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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:ACS32681.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ACS32681.1}.
SQ SEQUENCE 445 AA; 49638 MW; E921FA45877C73E3 CRC64;
MVVRPNVKEL PGPKAREVIE RNFKYLAMTT QDPENLPIVI ERGEGIRVYD VDGNVFYDFA
SGVGVINVGH AHPRVVEAIK KQAEKFTHYS LTDFFYENAV VLAEKLIELA PGDFEKKVVY
SNSGAEANEA AMKLVKYGTG RKQFLAFYHA FHGRTQAVLS LTASKWVQQD GFFPTMPGVT
HIPYPNPYRN TWGIDGYDEP DELINRVLDF IEEYVFRHVP PHEVGAIFFE PIQGEGGYVV
PPKNFFKELK KFADEYGILL ADDEVQMGIG RTGKFWAIEH FGVEPDLIQF GKAIGGGLPL
AGVVHRKEIS FDKPGRHATT FGGNPVAIAA GIEVVEIVKE LLPHVQEVGD YLHKILEELK
ENYEVIGDAR GLGLAQAVEI VKSKDTKEKY PELRDRIVGE AAKRGLVLLG CGDNSIRFIP
PLIVTKEEID IAMEIFEDAL KAALK
//
