QUTD_NEOFI
ID QUTD_NEOFI Reviewed; 542 AA.
AC A1D2R3;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Probable quinate permease;
DE AltName: Full=Quinate transporter;
GN Name=qutD; ORFNames=NFIA_013960;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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).
CC -!- FUNCTION: Integral membrane transporter that imports quinic acid to be
CC catabolized as a carbon source. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with creB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell
CC membrane {ECO:0000305}.
CC -!- PTM: Ubiquitinated. Deubiquitinated by creB, probably to control its
CC activity or amount.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; DS027688; EAW22706.1; -; Genomic_DNA.
DR RefSeq; XP_001264603.1; XM_001264602.1.
DR AlphaFoldDB; A1D2R3; -.
DR SMR; A1D2R3; -.
DR STRING; 36630.CADNFIAP00001188; -.
DR EnsemblFungi; EAW22706; EAW22706; NFIA_013960.
DR GeneID; 4591697; -.
DR KEGG; nfi:NFIA_013960; -.
DR VEuPathDB; FungiDB:NFIA_013960; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_12_1; -.
DR OMA; KVQWRFF; -.
DR OrthoDB; 430696at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0019630; P:quinate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Quinate metabolism; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..542
FT /note="Probable quinate permease"
FT /id="PRO_0000395719"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..66
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..325
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..387
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..542
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 519..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 60326 MW; 13562CE93BFF2D44 CRC64;
MSILALVEDR PTPKEVYNWR IYLLAAVASF TSCMIGYDSA FIGTTLALSS FREEFGFNTM
SKTAVNLVSA NIVSCYQAGA FFGAFLAYPV GHFWGRKWGL LFSGAIFTLG AGLMLGADGD
RGLGLLYGGR VLAGLGVGAG SNITPIYISE MAPPSIRGRL VGVYELGWQI GGLVGFWINY
GVSETLAPSH KQWIIPFAVQ LIPSGLLLIG AVFLKESPRW LFSRGRREDA IKNLCWIRQL
PADHIYMIEE IGAVDQALEE QRATIGLGFW KPFKAAGTNK KVMYRLFLGS MLFFWQNGSG
INAINYYSPT VFKSIGLQGA NTSMFSTGIF GVVKTVVTFV WLLYLIDRLG RRLLLLIGAA
GASVCLFIVG AYIKIADPAS NPTQEMTGGG IAAMFFFYLY TVFYTPSWNG TPWVMNSEMF
EPNMRSLAQA CAAASNWFWN FLISRFTPQM FAKMEYGVWF FFASLMVLSI VFVFFLLPET
KGIPLESMDA LFESRPIWRA HETVLARLRE DEERFRHDIE ESGYSKTGDQ QVEHLSEDLP
KV
