ID   NIA_EMENI               Reviewed;         873 AA.
AC   P22945; C8VU60; Q5BEM4;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   02-SEP-2026, entry version 160.
DE   RecName: Full=Nitrate reductase [NADPH];
DE            Short=NR;
DE            EC=1.7.1.3;
GN   Name=niaD; ORFNames=AN1006;
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; Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2205530; DOI=10.1016/0378-1119(90)90178-t;
RA   Johnstone I.L., McCabe P.C., Greaves P., Gurr S.J., Cole G.E., Brow M.A.D.,
RA   Unkles S.E., Clutterbuck A.J., Kinghorn J.R., Innis M.A.;
RT   "Isolation and characterisation of the crnA-niiA-niaD gene cluster for
RT   nitrate assimilation in Aspergillus nidulans.";
RL   Gene 90:181-192(1990).
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).
CC   -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC       of nitrate assimilation in plants, fungi and bacteria.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=nitrite + NADP(+) + H2O = nitrate + NADPH + H(+);
CC         Xref=Rhea:RHEA:19061, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.7.1.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 1 heme group. The heme group is called cytochrome b-557.
CC       {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the nitrate reductase family. {ECO:0000305}.
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DR   EMBL; M58291; AAA33314.1; -; Genomic_DNA.
DR   EMBL; AACD01000015; EAA65574.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF88350.1; -; Genomic_DNA.
DR   PIR; JH0182; JH0182.
DR   RefSeq; XP_658610.1; XM_653518.1.
DR   AlphaFoldDB; P22945; -.
DR   SMR; P22945; -.
DR   STRING; 227321.P22945; -.
DR   EnsemblFungi; CBF88350; CBF88350; ANIA_01006.
DR   GeneID; 2876780; -.
DR   KEGG; ani:ANIA_01006; -.
DR   VEuPathDB; FungiDB:AN1006; -.
DR   eggNOG; KOG0534; Eukaryota.
DR   eggNOG; KOG0535; Eukaryota.
DR   eggNOG; KOG0537; Eukaryota.
DR   HOGENOM; CLU_003827_4_0_1; -.
DR   InParanoid; P22945; -.
DR   OMA; KAMMPDY; -.
DR   OrthoDB; 432685at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; ISS:UniProtKB.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0050464; F:nitrate reductase (NADPH) activity; IDA:AspGD.
DR   GO; GO:0009061; P:anaerobic respiration; IMP:UniProtKB.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:InterPro.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
DR   CDD; cd06183; cyt_b5_reduct_like; 1.
DR   FunFam; 2.60.40.650:FF:000001; Nitrate reductase; 1.
DR   FunFam; 3.10.120.10:FF:000016; Nitrate reductase; 1.
DR   FunFam; 3.40.50.80:FF:000049; Nitrate reductase; 1.
DR   FunFam; 3.90.420.10:FF:000005; Nitrate reductase; 1.
DR   Gene3D; 2.60.40.650; -; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 3.90.420.10; Oxidoreductase, molybdopterin-binding domain; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR   InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR   InterPro; IPR012137; Nitr_rd_NADH.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR   InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR   InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19372:SF7; SULFITE OXIDASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR19372; SULFITE REDUCTASE; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF03404; Mo-co_dimer; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF00174; Oxidored_molyb; 1.
DR   PIRSF; PIRSF000233; Nitr_rd_NADH; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   PRINTS; PR00407; EUMOPTERIN.
DR   PRINTS; PR00371; FPNCR.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF56524; Oxidoreductase molybdopterin-binding domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum;
KW   NADP; Nitrate assimilation; Oxidoreductase; Reference proteome.
FT   CHAIN           1..873
FT                   /note="Nitrate reductase [NADPH]"
FT                   /id="PRO_0000166042"
FT   DOMAIN          512..587
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   DOMAIN          616..729
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          30..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         150
FT                   /ligand="Mo-molybdopterin"
FT                   /ligand_id="ChEBI:CHEBI:71302"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250|UniProtKB:P49050"
FT   BINDING         547
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   BINDING         570
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   BINDING         672..675
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT   BINDING         689..693
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT   BINDING         703..705
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT   BINDING         756
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT   BINDING         843..852
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   DISULFID        397
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   873 AA;  97560 MW;  BEE38281987A894C CRC64;
     MSTTVTQVRT GSIPKTLKTS QIRVEEQEIT ELDTADIPLP PPSKEPTEVL SLDKTTPDSH
     VPRDPRLIRL TGVHPFNVEP PLTALFQQGF LTPPELFYVR NHGPVPHVRD EDIPNWELRI
     EGLVEKPITL SFKQILQNYD QITAPITLVC AGNRRKEQNT VRKSKGFSWG SAALSTALFT
     GPMMADIIKS AKPLRRAKYV CMEGADNLPN GNYGTSIKLN WAMDPNRGIM LAHKMNGEDL
     RPDHGRPLRA VVPGQIGGRS VKWLKKLIIT DAPSDNWYHI YDNRVLPTMV TPDMSSQNPS
     WWRDERYAIY DLNVNSAAVY PQHKETLDLA AARPFYTAKG YAYAGGGRRI TRVEISLDKG
     KSWRLARIEY AEDKYRDFEG TLYGGRVDMA WREACFCWSF WSLDIPVSEL ASSDALLVRA
     MDEALSLQPK DMYWSVLGMM NNPWFRVKIT NENGRLLFEH PTDITGSSGW MEQIKKAGGD
     LTNGNWGERQ EGEEPVEAEP VVEVNMKKEG VTRIIDLEEF KKNSSDERPW FVVNGEVYDG
     TAFLEGHPGG AQSIISAAGT DASEEFLEIH SETAKKMMPD YHIGTLDKAS LEALRKGNAD
     TTDSSSDPRP TFLTPKAWTK ATLTKKTSVS SDTHIFTLSL EHPSQALGLP TGQHLMLKTP
     DPKSSSSGSI IRSYTPISPS DQLGMVDILI KIYAETPSIP GGKMTTALDT LPLGSVIECK
     GPTGRFEYLD RGRVLISGKE RFVKSFVMIC GGTGITPVFQ VLRAVMQDEQ DETKCVMLDG
     NRLEEDILLK NELDEFEALA GKKEKCKIVH TLTKGSESWT GRRGRIDEEL IRQHAGTPDR
     ETMVLVCGPE AMEKASKKIL LSLGWKEENL HYF
//