ID A2QBH1_ASPNC Unreviewed; 438 AA.
AC A2QBH1;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Contig An02c0010, genomic contig {ECO:0000313|EMBL:CAK96218.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:CAK96218.1};
GN ORFNames=An02g00030 {ECO:0000313|EMBL:CAK96218.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK96218.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK96218.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM269996; CAK96218.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QBH1; -.
DR EnsemblFungi; CAK96218; CAK96218; An02g00030.
DR VEuPathDB; FungiDB:An02g00030; -.
DR HOGENOM; CLU_017584_0_5_1; -.
DR Proteomes; UP000006706; Chromosome 4R.
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; 3.40.640.10; 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 PANTHER; PTHR42790; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42790:SF21; AROMATIC_AMINOADIPATE AMINOTRANSFERASE 1; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CAK96218.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Transferase {ECO:0000313|EMBL:CAK96218.1}.
FT DOMAIN 38..265
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 438 AA; 48879 MW; D9967194A1DA80D7 CRC64;
MISGLPHPSF FPFKIATVTA SPPTAEERPC LLELPLDGFL QYGSGTGNAQ LRAWCREFTQ
RVHRPAYADW TVLLHPGNTN AWSKVVSLLC ETDDYILCET YTYPSAQAFW IPLGIKAAPV
ASDAEGMRAD TLAQTLRDWE DTHPGTRRPR VLYLVSVGSN PSGVTMSTKR RRDVYDVCIE
YDVIIVEDDP YFFLQYPEYN AADSVTEGPE FVGSDEFLRS LTPSMLQFDH QGRVIRLESF
SKTLAPGLRL GYFVANPLFT ERLLRATEVE TQDPSGLSQA LTLRLLQSWG IDGYLGWLQG
LGVEYCRRRD WMIDAFSQHF RVGYAAKATG TLVAHLGDVP IFSFVPPTGG MFIWACFNLA
QNPAFEQLRH DENVVDPEQV MADQLWRQFA EAKVSSSHVV SLNMQRTHLY PLTGSLNPGA
ILSSLAGAGQ GYNKCARS
//
