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Protein

Nitrate reductase [NADPH]

Gene

nit-3

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.

Catalytic activityi

Nitrite + NADP+ + H2O = nitrate + NADPH.

Cofactori

Protein has several cofactor binding sites:
  • FADBy similarityNote: Binds 1 FAD per subunit.By similarity
  • hemeBy similarityNote: Binds 1 heme group per subunit. The heme group is called cytochrome b-557.By similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Pathwayi: nitrate reduction (assimilation)

This protein is involved in the pathway nitrate reduction (assimilation), which is part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the pathway nitrate reduction (assimilation) and in Nitrogen metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi240 – 2401MolybdenumBy similarity
Metal bindingi652 – 6521Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi675 – 6751Iron (heme axial ligand)PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi952 – 96110NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrate assimilation

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding, Molybdenum, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13438.
BRENDAi1.7.1.3. 3627.
UniPathwayiUPA00653.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrate reductase [NADPH] (EC:1.7.1.3)
Short name:
NR
Gene namesi
Name:nit-3
ORF Names:NCU05298
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
Proteomesi
  • UP000001805 Componenti: Chromosome 4, Linkage Group IV

Organism-specific databases

EuPathDBiFungiDB:NCU05298.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi652 – 6521H → A: Little loss of enzyme activity. 1 Publication
Mutagenesisi675 – 6751H → A: Loss of enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 982982Nitrate reductase [NADPH]PRO_0000166046Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi499 – 499InterchainSequence analysis

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

Its expression is highly regulated and responds rapidly to nitrate induction and to nitrogen repression.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP08619.
SMRiP08619. Positions 116-592.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini617 – 69276Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini721 – 836116FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the nitrate reductase family.Curated
Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000252609.
InParanoidiP08619.
KOiK10534.
OrthoDBiEOG7N63XM.

Family and domain databases

Gene3Di2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR017927. Fd_Rdtase_FAD-bd.
IPR014756. Ig_E-set.
IPR005066. MoCF_OxRdtse_dimer.
IPR008335. Mopterin_OxRdtase_euk.
IPR001834. NADH-Cyt_B5_reductase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR000572. OxRdtase_Mopterin-bd_dom.
IPR022407. OxRdtase_Mopterin_BS.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF03404. Mo-co_dimer. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view]
PRINTSiPR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF63380. SSF63380. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08619-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAPALEQRQ SLHDSSERQQ RFTSLILPNG VGCSSREEPQ GSGGLLVPHN
60 70 80 90 100
DNDIDNDLAS TRTASPTTTD FSSSSSDDNS TTLETSVNYS HSSNTNTNTS
110 120 130 140 150
CPPSPITSSS LKPAYPLPPP STRLTTILPT DLKTPDHLIR DPRLIRLTGS
160 170 180 190 200
HPFNVEPPLT ALFEHGFLTP QNLHYVRNHG PIPSSVATPP ATINKEEDDS
210 220 230 240 250
LLNWEFTVEG LVEHPLKISV RELMDASKWD NVTYPVTLVC AGNRRKEQNV
260 270 280 290 300
LRKSKGFSWG AGGLSTALWT GVGLSEILAR AKPLTKKGGG ARYVCFEGAD
310 320 330 340 350
QLPNGTYGTS VKLAWAMDPN KGIMVAHKMN GENLHPDHGR PVRVVVPGQI
360 370 380 390 400
GGRSVKWLKR IVVTKGPSEN WYHVFDNRVL PTTVGPEESG EKTEEMERVW
410 420 430 440 450
RDERYAIYDL NVNSVICEPG HGEVVSLRGD EGAGTYRLRG YAYAGGGRRV
460 470 480 490 500
TRLEVTLDQG KSWRLAGIEY PEDRYREAQD GEELFGGRLD VSWRESCFCW
510 520 530 540 550
CFWDLEIPLS ELRKAKDVCI RAMDESLALQ PKEMYWSVLG MMNNPWFRVV
560 570 580 590 600
IHHEGDTLRF EHPTQPMLTS DGWMDRVKKE GGNLANGFWG EKVPGAEENV
610 620 630 640 650
VKEEPVKEIS MVDEKVTRLI TLEELRQHDG EEEPWFVVNG QVYNGTPFLE
660 670 680 690 700
GHPGGAASIT GAAGQDVTDE FLAIHSENAK AMMPTYHIGT LTPSAPAALK
710 720 730 740 750
SSSTSDPALS DPSRPIFLQS KTWNSAILTF KESVSPDTKI FHFALSHPAQ
760 770 780 790 800
SIGLPVGQHL MMRLPDPAKP TESIIRAYTP ISDGTLERGT LRVLVKIYYA
810 820 830 840 850
SPTEDIKGGQ MTQALDALAL GKAVEFKGPV GKFVYQGRGV CSVNGRERKV
860 870 880 890 900
KRFVMVCGGS GVTPIYQVAE AVAVDDQDGT ECLVLDGNRV EGDILMKSEL
910 920 930 940 950
DELVERAKPM GRCRVKYTLS RPGAEWEGLR GRLDKTMLER EVGEGDLRGE
960 970 980
TMVLLCGPEG MQNMVREVLK GMGWKDEDVL VF
Length:982
Mass (Da):108,433
Last modified:June 1, 1994 - v3
Checksum:iB7838C031B19687F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 4919VGCSS…LLVPH → AAAAAAEKNPRGAADYCPSD in EAA32833 (PubMed:12712197).CuratedAdd
BLAST
Sequence conflicti139 – 1391I → IP in EAA32833 (PubMed:12712197).Curated
Sequence conflicti696 – 6961P → L in EAA32833 (PubMed:12712197).Curated
Sequence conflicti869 – 8702AE → LR in EAA32833 (PubMed:12712197).Curated
Sequence conflicti910 – 9101M → E in EAA32833 (PubMed:12712197).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61303 Genomic DNA. Translation: CAA43600.1.
CM002239 Genomic DNA. Translation: EAA32833.1.
PIRiS16292.
RefSeqiXP_962069.1. XM_956976.2.

Genome annotation databases

EnsemblFungiiEFNCRT00000005055; EFNCRP00000005051; EFNCRG00000005048.
GeneIDi3878217.
KEGGincr:NCU05298.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61303 Genomic DNA. Translation: CAA43600.1.
CM002239 Genomic DNA. Translation: EAA32833.1.
PIRiS16292.
RefSeqiXP_962069.1. XM_956976.2.

3D structure databases

ProteinModelPortaliP08619.
SMRiP08619. Positions 116-592.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000005055; EFNCRP00000005051; EFNCRG00000005048.
GeneIDi3878217.
KEGGincr:NCU05298.

Organism-specific databases

EuPathDBiFungiDB:NCU05298.

Phylogenomic databases

HOGENOMiHOG000252609.
InParanoidiP08619.
KOiK10534.
OrthoDBiEOG7N63XM.

Enzyme and pathway databases

UniPathwayiUPA00653.
BioCyciMetaCyc:MONOMER-13438.
BRENDAi1.7.1.3. 3627.

Family and domain databases

Gene3Di2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR017927. Fd_Rdtase_FAD-bd.
IPR014756. Ig_E-set.
IPR005066. MoCF_OxRdtse_dimer.
IPR008335. Mopterin_OxRdtase_euk.
IPR001834. NADH-Cyt_B5_reductase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR000572. OxRdtase_Mopterin-bd_dom.
IPR022407. OxRdtase_Mopterin_BS.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF03404. Mo-co_dimer. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view]
PRINTSiPR00406. CYTB5RDTASE.
PR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
SUPFAMiSSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF63380. SSF63380. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS51384. FAD_FR. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nit-3, the structural gene of nitrate reductase in Neurospora crassa: nucleotide sequence and regulation of mRNA synthesis and turnover."
    Okamoto P.M., Fu Y.-H., Marzluf G.A.
    Mol. Gen. Genet. 227:213-223(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  2. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  3. "On the presence of a heme-binding domain homologous to cytochrome b5 in Neurospora crassa assimilatory nitrate reductase."
    Le K.H.D., Lederer F.
    EMBO J. 2:1909-1914(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PARTIAL PROTEIN SEQUENCE.
  4. "Molecular characterization of conventional and new repeat-induced mutants of nit-3, the structural gene that encodes nitrate reductase in Neurospora crassa."
    Okamoto P.M., Garrett R.H., Marzluf G.A.
    Mol. Gen. Genet. 238:81-90(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTANTS.
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  5. "Nitrate reductase of Neurospora crassa: the functional role of individual amino acids in the heme domain as examined by site-directed mutagenesis."
    Okamoto P.M., Marzluf G.A.
    Mol. Gen. Genet. 240:221-230(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.

Entry informationi

Entry nameiNIA_NEUCR
AccessioniPrimary (citable) accession number: P08619
Secondary accession number(s): Q7RVF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 1, 1994
Last modified: July 6, 2016
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.