ID A2QA58_ASPNC Unreviewed; 419 AA.
AC A2QA58;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE SubName: Full=Contig An01c0330, genomic contig {ECO:0000313|EMBL:CAK37210.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:CAK37210.1};
GN ORFNames=An01g10290 {ECO:0000313|EMBL:CAK37210.1};
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:CAK37210.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK37210.1, 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 -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00038048}.
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DR EMBL; AM269980; CAK37210.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QA58; -.
DR EnsemblFungi; CAK37210; CAK37210; An01g10290.
DR VEuPathDB; FungiDB:An01g10290; -.
DR HOGENOM; CLU_031002_0_1_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR PANTHER; PTHR12286:SF5; SACCHAROPINE DEHYDROGENASE-LIKE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR12286; UNCHARACTERIZED; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:CAK37210.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..127
FT /note="Saccharopine dehydrogenase NADP binding"
FT /evidence="ECO:0000259|Pfam:PF03435"
SQ SEQUENCE 419 AA; 46258 MW; 3E68F94187361837 CRC64;
MNRPYDLIVY GATGYVGSLV VQYLWTHGPP TLRWAVAGRN EQKLTTLVDS LDRSNSLHQL
PHIMVAINSD KDLRYMASQT RLVLNTVGPF CKYGTPVVAA CIEHSTAYVD STGEPVWTQQ
LAAQWHDKAI ANRAIIIPHC AVAASPPDLM TLLLSRRIRQ PLGPVLFAIH HSWTGHSRGA
IESILAGLET YSPRQMMAAS SPLASCIPDA GPHRPHPTAP KLPVQRNRFL GDLTFNPSAV
ADQLVVMRTW SLLQRYGDPA ERYGDRFSYH GYTAASGWLQ AWSSFLVMSV ALVWIVLLPP
LRSLLRWLAP QPGKGPQLKH GEKHFVEWKA TVEAADRGGE PSVLGVMRMD TDVYSVCATL
VSEAGLTLLQ ILERKEEEVS LVKRLGGGIL TPASLGIQYV QRLEKAGLQW EVTDIKGKQ
//