ID Q0CQU9_ASPTN Unreviewed; 477 AA.
AC Q0CQU9;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN ORFNames=ATEG_03935 {ECO:0000313|EMBL:EAU35737.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU35737.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; CH476598; EAU35737.1; -; Genomic_DNA.
DR RefSeq; XP_001213113.1; XM_001213113.1.
DR AlphaFoldDB; Q0CQU9; -.
DR STRING; 341663.Q0CQU9; -.
DR EnsemblFungi; EAU35737; EAU35737; ATEG_03935.
DR GeneID; 4318345; -.
DR VEuPathDB; FungiDB:ATEG_03935; -.
DR eggNOG; KOG0257; Eukaryota.
DR HOGENOM; CLU_034385_1_0_1; -.
DR OMA; KNWRYPG; -.
DR OrthoDB; 5474881at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007963}.
FT DOMAIN 105..443
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 73..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 53327 MW; ADCF8E9F3FF784F7 CRC64;
MSFSGRRLSI LRPSNRRFSI GKELSENELR SETHRQFRTA HEGHRPHAGL DASRASTGVV
WCTERATEHG YAEDPSSWAN LGQGAPEADD EIEGSFPRPT SIPITSAARE YGPTAGIKPL
RAAVARLYNE HYRQGKQSQY TWENVCIVPG GRAGLIRIAA ILGNSYLSFP IPDYSAYSEM
LTLFKNIAPI PMPLAQDDHY HIHPDKIAEE IARGTSVLLT SNPRNPTGHT LSNEELIRIQ
DICRDRATLI LDEFYGGYNY TTDCDGSTIS GASNVEDVNK DDVLLIDGLT KRFRLPGWRI
AWVVGPKEFI DALGSAGSYL DGGANAPFQE AAVPMLEPSL VRAEMKALQQ HFREKRDYVL
KRLHEIGFRV KDVPQATFYI WLDLTSLEPP LPPKANISDG LNFFNALLRE KVIVVPGIFF
DLNPAKRRDL FDSPCHHFVR LSYGPKMDVL KKGLDGIENV VRRAREEFAV DEVAVDD
//
