HXNY_EMENI
ID HXNY_EMENI Reviewed; 349 AA.
AC C8VK14;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=2-oxoglutarate-Fe(II) type oxidoreductase hxnY {ECO:0000305};
DE EC=1.14.11.- {ECO:0000255|PROSITE-ProRule:PRU00805};
DE AltName: Full=Nicotinate catabolism cluster protein hxnY {ECO:0000303|PubMed:29212709};
GN Name=hxnY {ECO:0000303|PubMed:29212709}; ORFNames=ANIA_11188;
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: 2-oxoglutarate-Fe(II) type oxidoreductase, part of the hnx
CC cluster involved in the purine degradation (PubMed:29212709). The
CC nicotinate hydroxylase hnxS accepts nicotinate as a substrate and
CC catalyzes the first step of nicotinate catabolism (PubMed:29212709).
CC The major facilitator-type transporters hxnP and hxnZ are probably
CC involved in the uptake of nicotinate-derived metabolites, and the
CC oxidoreductases hxnT and hxnY in the further metabolism of 6-OH
CC nicotinic acid (PubMed:29212709). {ECO:0000269|PubMed:29212709}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
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 iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; BN001306; CBF82386.1; -; Genomic_DNA.
DR AlphaFoldDB; C8VK14; -.
DR SMR; C8VK14; -.
DR STRING; 227321.C8VK14; -.
DR EnsemblFungi; CBF82386; CBF82386; ANIA_11188.
DR VEuPathDB; FungiDB:AN11188; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_6_3_1; -.
DR InParanoid; C8VK14; -.
DR OMA; KYAMAPG; -.
DR OrthoDB; 755305at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1905736; P:negative regulation of L-proline import across plasma membrane; IEA:EnsemblFungi.
DR GO; GO:1905589; P:positive regulation of L-arginine import across plasma membrane; IEA:EnsemblFungi.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..349
FT /note="2-oxoglutarate-Fe(II) type oxidoreductase hxnY"
FT /id="PRO_0000443344"
FT DOMAIN 178..282
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 263
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 273
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 349 AA; 39087 MW; 7277CD5B5F9F9FC7 CRC64;
MAPTAPPILD FSPFYGTDGA AKAKLVQQVR ESCEYNGFFQ ITGHRIPREL QVRVMDAAKR
FFALPLEEKM AIDKNLNSFN RGYELLRSQM LEVGTAPELK EGLYIGEEIG ADHPYYINGR
LNSGPNQWPA TVPDAQEFRE TSMEYYHAVY ELAKDVLAVL ALTLDVEESF FDPLTEGGVA
TMRMLHYPSQ PKDEDEKLNR GIGAHTDFGC ITLLLQDEVD GLQVLDAPSG QWLDVQPVLG
AYVVNLGDLM MRMANDRYKS NIHRVINKSG RERYSIPFFF SGNPDHVCKC LPNCCKAGEQ
PKYPPITVED MVRGAYKQSY GRAEAYKKEL AEKAKAHKIE AASATAMVS
