ID Q8ZZ90_PYRAE Unreviewed; 315 AA.
AC Q8ZZ90;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=PAE0377 {ECO:0000313|EMBL:AAL62751.1};
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306 {ECO:0000313|EMBL:AAL62751.1, ECO:0000313|Proteomes:UP000002439};
RN [1] {ECO:0000313|EMBL:AAL62751.1, ECO:0000313|Proteomes:UP000002439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 /
RC IM2 {ECO:0000313|Proteomes:UP000002439};
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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}.
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DR EMBL; AE009441; AAL62751.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZZ90; -.
DR SMR; Q8ZZ90; -.
DR STRING; 178306.PAE0377; -.
DR EnsemblBacteria; AAL62751; AAL62751; PAE0377.
DR KEGG; pai:PAE0377; -.
DR PATRIC; fig|178306.9.peg.285; -.
DR eggNOG; arCOG04273; Archaea.
DR HOGENOM; CLU_017584_3_2_2; -.
DR InParanoid; Q8ZZ90; -.
DR Proteomes; UP000002439; 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; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR42885:SF1; THREONINE-PHOSPHATE DECARBOXYLASE; 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:AAL62751.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000002439};
KW Transferase {ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 28..309
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 315 AA; 34356 MW; 3667AFCC38F08E7A CRC64;
MPILTGVIAV CAAMHGGSSW ADPPVPDFSD NSNPLGPPRE LIRLVKEAVE RMAYLKFPAN
LVEEALSEYE GVEVTAFNGA TEALTVLLAS LRPRRVLIEW PNYTDYGRIA ELIGAEYVYV
DNFNSAGPGD VVIISNPNNP TGRLRKREEV LDLAGQLERR GAVLVVDESF IDFTSEPSAA
PDVLVVKSYG KFLAAPGLRL GGILGRVRGA LKAPWRVNSI ADYAVFHLGA SAMRRHREAT
VKYVAEESPR VQRELGKCAS VVPSPVHFFI VKGPMPQGVK VRPLTTHGIE GAYRVSIKTR
ELNDVLIKAV CREVS
//
