HXNP_EMENI
ID HXNP_EMENI Reviewed; 495 AA.
AC C8VJW1;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Major facilitator-type transporter hxnP;
DE AltName: Full=Nicotinate catabolism cluster protein hxnP {ECO:0000303|PubMed:29212709};
GN Name=hxnP {ECO:0000303|PubMed:29212709}; ORFNames=ANIA_11189;
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 [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 [2]
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 [3]
RP IDENTIFICATION, INDUCTION, AND FUNCTION.
RX PubMed=29212709; DOI=10.1098/rsob.170199;
RA Amon J., Fernandez-Martin R., Bokor E., Cultrone A., Kelly J.M.,
RA Flipphi M., Scazzocchio C., Hamari Z.;
RT "A eukaryotic nicotinate-inducible gene cluster: convergent evolution in
RT fungi and bacteria.";
RL Open Biol. 7:0-0(2017).
CC -!- FUNCTION: Major facilitator-type transporter, part of the hnx cluster
CC involved in the purine degradation (PubMed:29212709). The nicotinate
CC hydroxylase hnxS accepts nicotinate as a substrate and catalyzes the
CC first step of nicotinate catabolism (PubMed:29212709). The major
CC facilitator-type transporters hxnP and hxnZ are probably involved in
CC the uptake of nicotinate-derived metabolites, and the oxidoreductases
CC hxnT and hxnY in the further metabolism of 6-OH nicotinic acid
CC (PubMed:29212709). {ECO:0000269|PubMed:29212709}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:29212709};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced by nicotinate and 6-OH nicotinate,
CC subject to nitrogen metabolite repression mediated by the GATA factor
CC areA, and strictly regulated by the cluster-specific transcription
CC regulator hnxR (PubMed:29212709). {ECO:0000269|PubMed:29212709}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000255}.
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DR EMBL; BN001306; CBF82384.1; -; Genomic_DNA.
DR AlphaFoldDB; C8VJW1; -.
DR SMR; C8VJW1; -.
DR EnsemblFungi; CBF82384; CBF82384; ANIA_11189.
DR VEuPathDB; FungiDB:AN11189; -.
DR eggNOG; KOG2533; Eukaryota.
DR HOGENOM; CLU_001265_0_1_1; -.
DR InParanoid; C8VJW1; -.
DR OMA; YIPNGLC; -.
DR OrthoDB; 412158at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031224; C:intrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..495
FT /note="Major facilitator-type transporter hxnP"
FT /id="PRO_0000443342"
FT TRANSMEM 36..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 495 AA; 55114 MW; 6F021B5AD9C14CC3 CRC64;
MGATATDIEK VPSAGTPDEP KAGETNVYVD TEAEKSFVRK VDFFVLPMLC LMYFFDCMDR
SNLANAKTDG LEEDINLKGN EYSLLILLFY IPFGLFDLPW NLLIKRYSAR IMLSLRRYAV
TVVWGICALC QCAANNFGGL LAIRIILGVF EAGFFAGSTF YFTLFYTRNE MGFRLAVLQS
FAVLASAFSG LISFGLFQIN HSAVKGWQWL FIVEGAMTLI IGVIGFWWLP DTAQSAWFLT
QRERDAASAR LLRDTSAEIE TKLELKAAFQ TWSDWKFPIW AVITFSYPVA YATAMNFFPI
IVARLGYSVV KTNLWTVAPN LVGAVVLLVV AKSSDIFRER SLHIIFSLTV SLVGMLILAS
IDVSHNKGVS YFACFLLASG AYIPTCLVHA WHNNNNTNEN SRAANTGFFV GLGNIAGVLS
AATFRTEYAP KYVPTLVATC ACNGVCILAT AFMGTWMRLE NRRKDKEQGA RIVAGQVETR
MLADGEKSPE WRYFL
