QUTD_ASPNC
ID QUTD_ASPNC Reviewed; 539 AA.
AC A2QQV6;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Probable quinate permease;
DE AltName: Full=Quinate transporter;
GN Name=qutD; ORFNames=An08g03850;
OS Aspergillus niger (strain 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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
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.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.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 -!- 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; AM270166; CAK39888.1; -; Genomic_DNA.
DR RefSeq; XP_001392502.1; XM_001392465.2.
DR AlphaFoldDB; A2QQV6; -.
DR SMR; A2QQV6; -.
DR PaxDb; A2QQV6; -.
DR EnsemblFungi; CAK39888; CAK39888; An08g03850.
DR GeneID; 4982700; -.
DR KEGG; ang:ANI_1_1882074; -.
DR VEuPathDB; FungiDB:An08g03850; -.
DR HOGENOM; CLU_001265_30_12_1; -.
DR Proteomes; UP000006706; Chromosome 8R.
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..539
FT /note="Probable quinate permease"
FT /id="PRO_0000395716"
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..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..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..539
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 539 AA; 60479 MW; 81B70C5EC37D1C5C CRC64;
MSILSMVEDR PTPKEVYNWR IYLLAAVASF TSCMIGYDSA FIGTTISLDS FKNEFHWDSM
STAKQNLVSA NIVSCYQAGA FFGAFFAYPI GHFWGRKWGL MLSALVFTLG AGLMLGANGD
RGLGLIYGGR VLAGLGVGAG SNFTPIYISE LAPPAIRGRL VGVYELGWQV GGLVGFWINY
GVEQTMAPSH KQWLIPFAVQ LIPAGLLIIG ILFVKESPRW LFLRGRREEA IKNLCWIRQI
PADHIYMIEE IGAIDQTLEH QRSTIGLGFW RPLKEAWTNK RILYRLFLGS MLFFWQNGSG
INAINYYSPT VFKSIGLKGN SSSLLTTGIF GVVKTVVTIV WLLYLIDHVG RRLLLLIGAA
GGSICMWIVG AYIKVVDPTH NQSDHLNGGG VAAIFFFYLW TAFYTPSWNG TPWVINSEMF
DPNIRSLAQA CAAGSNWLWN FLISRFTPQM FAKMDYGVYF FFASLMLLSI PFVFFLVPET
KGIPLENMDP LFQTQPVWRA HAKVLAQIHE DEARFRRDLE ESGYTKGNVE QVEDTDRKE
