ID A1CP17_ASPCL Unreviewed; 439 AA.
AC A1CP17;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Aminotransferase, putative {ECO:0000313|EMBL:EAW07388.1};
GN ORFNames=ACLA_020960 {ECO:0000313|EMBL:EAW07388.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW07388.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW07388.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027059; EAW07388.1; -; Genomic_DNA.
DR RefSeq; XP_001268814.1; XM_001268813.1.
DR AlphaFoldDB; A1CP17; -.
DR STRING; 344612.A1CP17; -.
DR EnsemblFungi; EAW07388; EAW07388; ACLA_020960.
DR GeneID; 4701399; -.
DR KEGG; act:ACLA_020960; -.
DR VEuPathDB; FungiDB:ACLA_020960; -.
DR eggNOG; KOG0634; Eukaryota.
DR HOGENOM; CLU_017584_0_6_1; -.
DR OMA; MIALDSM; -.
DR OrthoDB; 850at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42858; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42858:SF1; LD15494P; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:EAW07388.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Transferase {ECO:0000313|EMBL:EAW07388.1}.
FT DOMAIN 39..424
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 439 AA; 48175 MW; 6DDB796C2B0DCFBF CRC64;
MDSVIDLSRG WPNPALLPTT ALANASATVL STPSIWTPAL LYGPDPGYEP LRQAVAQWLT
SFYHPRHPIT SNRICITGGA SQNLACIFQV FTDPSYTRNV WMVAPTYQLA SRMVDDAGFA
GRMRVIPQDA TGLDLAFLRR ELEVAEEKAN AEHRSEPKLK PPRPWGKIYK HVIYAIPTFS
NPSTLTMSQS DRESLVQLAR DFDALIVTDD VYDFLQWSAD PNAPLSTPHK APEPRLVDVD
AYLDGGPKDE WGNVVSNGSF SKLIGPGMRT GWAEGTAKFA YGLSQTGSSR SGGAPSQMAS
TIVAQLLETG AFQTHLAQVL LPAYARRYHR LMSAVREHLV PVGAAPRESS RVAGGYFIWV
RLPAPLRARD LARTALEKHQ VNVAPGEIFQ VPGDSEHGAN DFCDHLRLCF AWVEEEQLAE
GVCRLGRAIR EALESSGKL
//
