ID N0BJ29_9EURY Unreviewed; 376 AA.
AC N0BJ29;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=Asulf_00134 {ECO:0000313|EMBL:AGK60170.1};
OS Archaeoglobus sulfaticallidus PM70-1.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=387631 {ECO:0000313|EMBL:AGK60170.1, ECO:0000313|Proteomes:UP000013307};
RN [1] {ECO:0000313|EMBL:AGK60170.1, ECO:0000313|Proteomes:UP000013307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM70-1 {ECO:0000313|EMBL:AGK60170.1};
RX PubMed=23833130;
RA Stokke R., Hocking W.P., Steinsbu B.O., Steen I.H.;
RT "Complete Genome Sequence of the Thermophilic and Facultatively
RT Chemolithoautotrophic Sulfate Reducer Archaeoglobus sulfaticallidus Strain
RT PM70-1T.";
RL Genome Announc. 1:e00406-13(2013).
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|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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DR EMBL; CP005290; AGK60170.1; -; Genomic_DNA.
DR RefSeq; WP_015589769.1; NC_021169.1.
DR AlphaFoldDB; N0BJ29; -.
DR STRING; 387631.Asulf_00134; -.
DR GeneID; 15391780; -.
DR KEGG; ast:Asulf_00134; -.
DR eggNOG; arCOG01130; Archaea.
DR HOGENOM; CLU_017584_4_3_2; -.
DR OrthoDB; 372018at2157; -.
DR Proteomes; UP000013307; 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:SF1; ASPARTATE AMINOTRANSFERASE; 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:AGK60170.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013307};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:AGK60170.1}.
FT DOMAIN 30..371
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 376 AA; 42091 MW; 773AC4B62D2349E4 CRC64;
MITKRVNAVS PSATLRVSEL AKKLRREGNP VIDMSVGEPD FPTPSFIIEA AYKAMKEGKV
FYTPTRGIPE LLSAISEKLK NENGLDYAPE NIITTPGAKY AIYEAIMAVV EEGDEVILLD
PSWVTYEACI KMAGGKVVWV PHAEGFEDAP VEDYITSKTK LIIINSPSNP LGVVYPESFL
KKIRDLAVDR NILVMSDEVY EKIIFDGKHK SIAEFDGMLE RTILINGLSK TYSMTGWRLG
YAASTEEIIK AMTKIQSHSV SHPTSFVQYA AVAAIKSDQS FLNEMVSEFK ARRDIIMDGL
DRLGIKYAPP KGAFYIFMDV KQDSMKFCEE FLAKEYVATT PGSAFGLKYS TWVRVSYATS
RENIEEMLVR LERFLS
//
