ID   HXNZ_EMENI              Reviewed;         553 AA.
AC   C8VK15;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Major facilitator-type transporter hxnZ {ECO:0000303|PubMed:29212709};
DE   AltName: Full=Nicotinate catabolism cluster protein hxnZ {ECO:0000303|PubMed:29212709};
GN   Name=hxnZ {ECO:0000303|PubMed:29212709}; ORFNames=ANIA_11196;
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; CBF82387.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8VK15; -.
DR   SMR; C8VK15; -.
DR   EnsemblFungi; CBF82387; CBF82387; ANIA_11196.
DR   VEuPathDB; FungiDB:AN11196; -.
DR   eggNOG; KOG0253; Eukaryota.
DR   HOGENOM; CLU_001265_52_2_1; -.
DR   InParanoid; C8VK15; -.
DR   OMA; VQMFFSV; -.
DR   OrthoDB; 1430447at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 1.
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..553
FT                   /note="Major facilitator-type transporter hxnZ"
FT                   /id="PRO_0000443343"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        433..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        459..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        496..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        525..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   553 AA;  60145 MW;  3497F3E1030F8972 CRC64;
     MDISYPVINA GGLKNIASQI IMEIELDKRE NRPTDNVPPD DIGKIEVVDD AEMEQFYGSS
     TTDAYRLKSE LVSQCMADIG MGRFQWKLFT VAGFGWIVDN FCSQGISAVQ PPIQQEFSGI
     KQVSYSSVAY YVGMIIGASF WGISSDLIGR KPAFNSTLAI AGIFLCAAAG TSNFIAFSAL
     WAVIGTAAGG NVVCDSMILL EFIPGSHQYL LTALSGWWNL GQLVVSLLAW VFLANFSCPT
     DATPDTCSRA DNMGWRYTLI TLGGLSLAFT FVRIFVFKMP ETPRYLLSQG NDQAAVDAVN
     YVARQNGKPE PLTLSMLQAI DVRLGFTPNA EERLSTKDIL KENMQEFRGE HYQALFATRK
     LSQHTALIWA VWLIIGIAYP LYFNFLPSYL ATRFTQDSSL DLTYRNYCIQ SAVGVVGPLS
     AAVLVNTFLG RRWMMGISSI VTGVFLFAYV GVKTPMSSLA FSCVTGLLAN FANQLSEYAI
     MYAFTPESFP APHRGTASGT AASLLRFGGL VASLIASETG FTTAPIYASA ALWVGVGVLC
     FGLPFETHGH AAI