ID B0XQS7_ASPFC Unreviewed; 366 AA.
AC B0XQS7;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Quinate utilisation oxidoreductase QutH {ECO:0000313|EMBL:EDP56391.1};
GN ORFNames=AFUB_011010 {ECO:0000313|EMBL:EDP56391.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP56391.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP56391.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
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; DS499594; EDP56391.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XQS7; -.
DR EnsemblFungi; EDP56391; EDP56391; AFUB_011010.
DR VEuPathDB; FungiDB:AFUB_011010; -.
DR HOGENOM; CLU_023194_1_1_1; -.
DR PhylomeDB; B0XQS7; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43377; BILIVERDIN REDUCTASE A; 1.
DR PANTHER; PTHR43377:SF1; BILIVERDIN REDUCTASE A; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 3..115
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 136..363
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 366 AA; 39517 MW; 162A8F9EE3FC0889 CRC64;
MPLRIIIVGA GLIGPRHAQS VLSNPSTELV ALVDPASSGA RVASQLQTEH FPSVPAMLAA
IPKPDAAIIC TPNHTHVPIA TELLSHGIHI LTEKPLSDSV ESAQSLLAFA RRPENAHLTV
LVGHHRRFNP YVRAAKEILD SNSLGTVIAV NGLWTLYKPE AYFAPPTDWR RVRPSGGVIP
INLVHDIDTL QYLFGPITRV HAERTPRQRA NPPHEVEEGA ALILRFASGV VGTFLVCDAT
PSPHNFEMGT GENPLIPGPP GASEGGGGAD FYRIFGSEAC LSVPDMTRWS YDGRAEKSWT
EQLAVERLEV DQKAAPFDLQ LAHFVEVIAG REPPRCSGED GLRALMVCEG VRRALETGEA
VDLPVI
//