NIA_USTMA
ID NIA_USTMA Reviewed; 983 AA.
AC Q05531; A0A0D1DXC6; Q4P7R6; Q96VE8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Nitrate reductase [NADPH];
DE Short=NR;
DE EC=1.7.1.3;
GN Name=NAR1; ORFNames=UMAG_03847;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=8370542; DOI=10.1016/0378-1119(93)90670-x;
RA Banks G.R., Holden D.W., Kanuga N., Shelton P., Spanos A.;
RT "The Ustilago maydis nar1 gene encoding nitrate reductase activity:
RT sequence and transcriptional regulation.";
RL Gene 131:69-78(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FBD11;
RX PubMed=11737646; DOI=10.1046/j.1365-2958.2001.02699.x;
RA Brachmann A., Weinzierl G., Kaemper J., Kahmann R.;
RT "Identification of genes in the bW/bE regulatory cascade in Ustilago
RT maydis.";
RL Mol. Microbiol. 42:1047-1063(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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=H2O + NADP(+) + nitrite = H(+) + NADPH + nitrate;
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 per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 1 heme group per subunit. The heme group is called
CC cytochrome b-557. {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 -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INDUCTION: Its expression is highly regulated and responds rapidly to
CC nitrate induction and to ammonium ion repression.
CC -!- SIMILARITY: Belongs to the nitrate reductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA47918.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X67687; CAA47918.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AJ315577; CAC41650.1; -; Genomic_DNA.
DR EMBL; CM003149; KIS68266.1; -; Genomic_DNA.
DR PIR; JN0804; JN0804.
DR RefSeq; XP_011390279.1; XM_011391977.1.
DR AlphaFoldDB; Q05531; -.
DR SMR; Q05531; -.
DR STRING; 5270.UM03847P0; -.
DR EnsemblFungi; KIS68266; KIS68266; UMAG_03847.
DR GeneID; 23564194; -.
DR KEGG; uma:UMAG_03847; -.
DR VEuPathDB; FungiDB:UMAG_03847; -.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_003827_4_0_1; -.
DR InParanoid; Q05531; -.
DR OMA; TAKAMMP; -.
DR OrthoDB; 166846at2759; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000000561; Chromosome 10.
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; IEA:UniProtKB-EC.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.10.120.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR Gene3D; 3.90.420.10; -; 1.
DR InterPro; IPR001834; CBR-like.
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; 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; PTHR19370; PTHR19370; 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 PRINTS; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00407; EUMOPTERIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR SUPFAM; SSF56524; SSF56524; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR SUPFAM; SSF81296; SSF81296; 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 2: Evidence at transcript level;
KW FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NADP;
KW Nitrate assimilation; Oxidoreductase; Reference proteome.
FT CHAIN 1..983
FT /note="Nitrate reductase [NADPH]"
FT /id="PRO_0000166048"
FT DOMAIN 585..662
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 688..815
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 184
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 622
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 645
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 746..749
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 763..767
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 768
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 780
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 784..786
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 841
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 844
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 952..961
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT CONFLICT 5
FT /note="T -> S (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 18..20
FT /note="KGD -> NP (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="V -> I (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="H -> Q (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..179
FT /note="LP -> PT (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 243..244
FT /note="PG -> LD (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="G -> S (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="K -> Q (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="A -> S (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="Q -> E (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="H -> R (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="Q -> E (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="G -> V (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="M -> Q (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="Missing (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="G -> V (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 572..573
FT /note="VD -> WV (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="V -> L (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="D -> DD (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 673..675
FT /note="TEG -> ER (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 726..733
FT /note="HVFVRVRS -> QLCVCRL (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="T -> A (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 894..895
FT /note="LR -> M (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 927
FT /note="T -> S (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
FT CONFLICT 970..971
FT /note="KQ -> NE (in Ref. 1; CAA47918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 983 AA; 108826 MW; E8BF3D172EEB69B9 CRC64;
MTISTTSSST SSKTSSEKGD DLKGFSSSSS PASSRSSSAT TPEPSSPTVL AAKTIESIDP
FQPRKDYNEN VLPAIPATEA VQPLTSDANT PDHWIARDER MIRLTGKHPF NSEAPLSELF
SKGFLTPQNL FYVRSHGDTP RVTREQAENW KLKVHGLVEQ EVELSIKDLK EKFPTVTLPI
TLVCAGNRRK EQNMVAKGLG FNWGAAGVST GLFTGVYLAD ILDYCKPKNP LLSSFPSYDV
AVPGRARHVV FEGADELPKG KYGTSQRLNW ALDRCKGMLI AWGLNGEDLS PDHGYPLRLV
VPGQIGGRMV KWLERIEVSD RESQHHLHFH DNKVLPTEVT ADQARSEMHW WYDPKYIIND
LNVNAAICSP DHDQVVNVAE PSTSSPQMLP LEGYAYTGGG RRIHRVEISL DDGHSWKCAS
IHYPEDLYRM YPIQGHEYFG TLDLSATEMS FSWCFWRLDV DVQADIIAKD VKVISVRALD
EGLATMPRDM YWNATSMMNS WWFRVAVHRE GENGNQIRFE HPTLAGNAPG GWMQRMNEAG
LNPRYPQFGE AKAVESCKTD ANTLAAAKEA KVDPKAIMID PSKADTIITA ADLAAHGDGE
GPEPWFVVHG HVYDGTGFLK DHPGGDQSIR LVAGEDATED FMAIHSMDAK KMLRDFHLGR
LEKQDAAPPA ATTEGEVLDL SKPFLDPKKW RATRLVSKQI ISPDARIFRF ALGSEDQELG
LPVGQHVFVR VRSKNARTGE TEMVQRAYTP YSGNTQRGFL DILIKVYFPS DAAATSAPAF
EGGKMTMLLE KIDVSSPSDD LTIELKGPLG SFTYLGQQQI RWKPASAVRR VRKLAMIAGG
SGITPIWSTL KAIADEVLDA SNPSSPALDP IQIWIVYGNR TEQDILIREE LERLRVALKG
NLKVWHVLSN CTPENEANWS MGRGHITANV LRTHLPPPPA KPASEDELED TLALVCGPPP
MEKAVSDGLK QLGWDLQRCV VFF
