QUTD_EMENI
ID QUTD_EMENI Reviewed; 533 AA.
AC P15325; C8VTA9; Q5BE92;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Quinate permease;
DE AltName: Full=Quinate transporter;
GN Name=qutD; ORFNames=AN1138;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2976880; DOI=10.1007/bf00337715;
RA Hawkins A.R., Lamb H.K., Smith M., Keyte J.W., Roberts C.F.;
RT "Molecular organisation of the quinic acid utilization (QUT) gene cluster
RT in Aspergillus nidulans.";
RL Mol. Gen. Genet. 214:224-231(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP UBIQUITINATION, INTERACTION WITH CREB, AND DEUBIQUITINATION BY CREB.
RA Kamlangdee N.;
RT "Identifying target proteins of the CreB deubiquitination enzyme in the
RT fungus Aspergillus nidulans.";
RL Thesis (2008), University of Adelaide, Australia.
CC -!- FUNCTION: Integral membrane transporter that imports quinic acid to be
CC catabolized as a carbon source.
CC -!- SUBUNIT: Interacts with creB. {ECO:0000269|Ref.4}.
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. {ECO:0000269|Ref.4}.
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; X13525; CAA31879.1; -; Genomic_DNA.
DR EMBL; AACD01000016; EAA66256.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF88069.1; -; Genomic_DNA.
DR PIR; S08498; S08498.
DR RefSeq; XP_658742.1; XM_653650.1.
DR AlphaFoldDB; P15325; -.
DR SMR; P15325; -.
DR STRING; 162425.CADANIAP00001491; -.
DR EnsemblFungi; CBF88069; CBF88069; ANIA_01138.
DR EnsemblFungi; EAA66256; EAA66256; AN1138.2.
DR GeneID; 2876917; -.
DR KEGG; ani:AN1138.2; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_12_1; -.
DR InParanoid; P15325; -.
DR OMA; KVQWRFF; -.
DR OrthoDB; 430696at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell membrane; Membrane; Quinate metabolism; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..533
FT /note="Quinate permease"
FT /id="PRO_0000050448"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..67
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..324
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..346
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..385
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..454
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..533
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 75
FT /note="A -> R (in Ref. 1; CAA31879)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="P -> S (in Ref. 1; CAA31879)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="K -> T (in Ref. 1; CAA31879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 59428 MW; 9A6E78D6EA90B0F2 CRC64;
MSILALVEDR PTPREVYNWR VYLLAAVASF TSCMIGYDSA FIGTTLSLQS FQNEFNWESL
NTDLISANIV SLYQAGAFFG ALFAYPIGHF WGRRWGLMFS ALIFFLGAGM MLGANGDRGL
GLIYGGRVLA GIGVGAGSNI CPIYISEMAP PAIRGRLVGV YELGWQIGGV VGFWINYGVD
ETLAPSHKQW IIPFAVQLIP AGLLIIGALL IRESPRWLFL RGNREKGIET LAWIRNLPAD
HIYMVEEINM IEQSLEQQRV KIGLGFWKPF KAAWTNKRIL YRLFLGSMLF LWQNGSGINA
INYYSPRVFK SIGVSGGNTS LLTTGIFGVV KAVITFVWLL YLIDHFGRRN LLLVGAAGGS
VCLWIVGGYI KIAKPENNPE GTQLDSGGIA AIFFFYLWTA FYTPSWNGTP WVINSEMFDP
TVRSLAQACA AASNWLWNFL ISRFTPQMFT SMGYGVYFFF ASLMILSIVF VFFLIPETKG
VPLESMETLF DKKPVWHAHS QLIRELRENE EAFRADMGAS GKGGVTKEYV EEA
