ID C5A1S1_THEGJ Unreviewed; 392 AA.
AC C5A1S1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=aspC-3 {ECO:0000313|EMBL:ACS34340.1};
GN OrderedLocusNames=TGAM_1838 {ECO:0000313|EMBL:ACS34340.1};
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117 {ECO:0000313|EMBL:ACS34340.1, ECO:0000313|Proteomes:UP000001488};
RN [1] {ECO:0000313|EMBL:ACS34340.1, 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 ECO:0000256|RuleBase:RU000481};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR EMBL; CP001398; ACS34340.1; -; Genomic_DNA.
DR RefSeq; WP_015859449.1; NC_012804.1.
DR AlphaFoldDB; C5A1S1; -.
DR STRING; 593117.TGAM_1838; -.
DR PaxDb; 593117-TGAM_1838; -.
DR GeneID; 7987665; -.
DR KEGG; tga:TGAM_1838; -.
DR PATRIC; fig|593117.10.peg.1847; -.
DR eggNOG; arCOG01130; Archaea.
DR HOGENOM; CLU_017584_4_3_2; -.
DR OrthoDB; 372018at2157; -.
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 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 PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF3; ASPARTATE AMINOTRANSFERASE-RELATED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
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:ACS34340.1};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ACS34340.1}.
FT DOMAIN 34..384
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 392 AA; 45208 MW; B17C770B86C22DEB CRC64;
MKYKKRKYFL AGRINLIQRS KIRELFEKAR KMENVISLGI GEPDFDTPEV IKEAAKRALD
EGYTHYTPNA GIPEFREAIA EYYREFYKID VDVDSILVTA GAYEATYLAF ESLLEEGDDV
IIPDPAFVCY VEDAKISEAG IIRIPLREEN RFRIDPDELV ELITKRTRMI VINYPNNPTG
ATLDKETAKA IAQIAEDYNI YILSDEPYEH FLYEGARHYP MIKYAPDNTI LANSFSKTFA
MTGWRLGFAI APPQVIKDMI KLHAYIIGNV TSFIQIAGIT ALRDKRSWEA VENMRKIYAE
RRKLTLRYLN EMPHIEPFRP KGAFYVWAKI DPELDMSSED FAEWLLENAG VVVIPGTAFG
KHGEGWIRIS YATKKEQLIE AMERMRRALE KL
//
