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QUTD_ASPFN
ID   QUTD_ASPFN              Reviewed;         537 AA.
AC   B8NIM7;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable quinate permease;
DE   AltName: Full=Quinate transporter;
GN   Name=qutD; ORFNames=AFLA_068140;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963479; EED49992.1; -; Genomic_DNA.
DR   RefSeq; XP_002380373.1; XM_002380332.1.
DR   AlphaFoldDB; B8NIM7; -.
DR   SMR; B8NIM7; -.
DR   STRING; 5059.CADAFLAP00008238; -.
DR   EnsemblFungi; EED49992; EED49992; AFLA_068140.
DR   VEuPathDB; FungiDB:AFLA_068140; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   HOGENOM; CLU_001265_30_12_1; -.
DR   OMA; KVQWRFF; -.
DR   Proteomes; UP000001875; 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; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..537
FT                   /note="Probable quinate permease"
FT                   /id="PRO_0000395714"
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..537
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   537 AA;  60380 MW;  07AFC66810586F9C CRC64;
     MSILSLVEDR PTPKEVYNWK IYLLAAVASC TSCMIGYDSA FIGTTISLQS FKDEFDWDSM
     SAAHQDLVSS NIVSLYQAGA FFGAFFAYPI GHFWGRKWGL MVSALIFTLG AGIMLGTNGD
     RGFGLLYGGR VLAGLGVGAG SNITPIYISE LSPPAIRGRL VGVYELGWQI GGLVGFWICY
     GVDETLPPSH KQWIIPFAVQ LIPSGLLIIG ALFLKESPRW LFLRGRREEA IKNLCWIRQL
     PEDHVYMIEE IGAIDQTLEH QRATIGLGFW KPFAAAWTNK KILYRLFLGS MLFFWQNGSG
     INAINYYSPT VFKSIGVTGS NTSLFTTGIF GVVKTVVTFI WLLWLIDRVG RRLLLLIGAA
     GGSICLWIVG AYIKIARPSE RENKQMDGGG IAAMFFFYLW TVFYTPSWNG TPWVINSEMF
     DPNIRSLAQA CAAGSNWLWN FLISRFTPQM FAKMDYGVYF FFASLMILSI IFVFFLIPET
     KGIPLESMDR LFETQPIWRA HGTLLKQIRE DEERFRHDLE DSGFVKSTDR QVEVVDA
 
 
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