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UniProtKB/Swiss-Prot entry P08619


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NIA_NEUCR
Primary accession number P08619
Secondary accession number Q7RVF6
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on June 1, 1994 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 88)
Name and origin of the protein
Protein name Nitrate reductase [NADPH]
Synonyms NR
EC 1.7.1.3
Gene name
Name: nit-3
ORFNames: NCU05298
From
Neurospora crassa [TaxID: 5141] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
DOI=10.1007/BF00259673; PubMed=1829499 [NCBI, ExPASy, EBI, Israel, Japan]
Okamoto P.M., Fu Y.-H., Marzluf G.A.;
"Nit-3, the structural gene of nitrate reductase in Neurospora crassa: nucleotide sequence and regulation of mRNA synthesis and turnover.";
Mol. Gen. Genet. 227:213-223(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
DOI=10.1038/nature01554; PubMed=12712197 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
[3]
PRELIMINARY PARTIAL PROTEIN SEQUENCE AROUND HIS-652.
PubMed=16453480 [NCBI, ExPASy, EBI, Israel, Japan]
Le K.H.D., Lederer F.;
"On the presence of a heme-binding domain homologous to cytochrome b5 in Neurospora crassa assimilatory nitrate reductase.";
EMBO J. 2:1909-1914(1983).
[4]
MUTANTS.
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=8479443 [NCBI, ExPASy, EBI, Israel, Japan]
Okamoto P.M., Garrett R.H., Marzluf G.A.;
"Molecular characterization of conventional and new repeat-induced mutants of nit-3, the structural gene that encodes nitrate reductase in Neurospora crassa.";
Mol. Gen. Genet. 238:81-90(1993).
[5]
MUTAGENESIS.
DOI=10.1007/BF00277060; PubMed=8355655 [NCBI, ExPASy, EBI, Israel, Japan]
Okamoto P.M., Marzluf G.A.;
"Nitrate reductase of Neurospora crassa: the functional role of individual amino acids in the heme domain as examined by site-directed mutagenesis.";
Mol. Gen. Genet. 240:221-230(1993).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X61303; CAA43600.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AABX02000019; EAA32833.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S16292; S16292.
3D structure databases
HSSP P00171; 1M2M. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P08619.
Enzyme and pathway databases
BioCyc MetaCyc:MON-13438; -.
Ontologies
GO
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030151; Molecular function: molybdenum ion binding (inferred from electronic annotation from InterPro).
GO:0050464; Molecular function: nitrate reductase (NADPH) activity (inferred from electronic annotation from EC).
GO:0042128; Biological process: nitrate assimilation (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001199; Cyt_B5.
IPR001834; Cyt_B5_reductase.
IPR005066; MoCF_OxRdtse_dimer.
IPR008335; Mopterin_OxRdtase_euk.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR000572; OxRdtase_Mopterin-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.10.120.10; Cyt_B5; 1.
G3DSA:2.60.40.650; MoCF_oxrdtse_dimer; 1.
G3DSA:3.90.420.10; Oxred_molyb_bd; 1.
Pfam PF00173; Cyt-b5; 1.
PF00970; FAD_binding_6; 1.
PF03404; Mo-co_dimer; 1.
PF00175; NAD_binding_1; 1.
PF00174; Oxidored_molyb; 1.
Pfam graphical view of domain structure.
PRINTS PR00406; CYTB5RDTASE.
PR00363; CYTOCHROMEB5.
PR00407; EUMOPTERIN.
ProDom PD000612; Cyt_B5; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00191; CYTOCHROME_B5_1; 1.
PS50255; CYTOCHROME_B5_2; 1.
PS51384; FAD_FR; 1.
PS00559; MOLYBDOPTERIN_EUK; 1.
PROSITE graphical view of domain structure (profiles).
Other
ProtoNet P08619.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NADP; Nitrate assimilation; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   982  982     Nitrate reductase [NADPH]. PRO_0000166046
DOMAIN   617   692  76     Cytochrome b5 heme-binding. 
DOMAIN   721   836  116     FAD-binding FR-type. 
NP_BIND   952   961  10     NADP (By similarity). 
METAL   240   240        Molybdenum-pterin (Potential). 
METAL   295   295        Molybdenum-pterin (Potential). 
METAL   652   652        Iron (heme axial ligand) (By similarity). 
METAL   675   675        Iron (heme axial ligand) (By similarity). 
DISULFID   499   499        Interchain (Potential). 
MUTAGEN   652   652        H->A: Little loss of enzyme activity. 
MUTAGEN   675   675        H->A: Loss of enzyme activity. 
CONFLICT   31    49        VGCSSREEPQGSGGLLVPH -> AAAAAAEKNPRGAADYCPSD (in Ref. 2; EAA32833). 
CONFLICT   139   139        I -> IP (in Ref. 2; EAA32833). 
CONFLICT   696   696        P -> L (in Ref. 2; EAA32833). 
CONFLICT   869   870        AE -> LR (in Ref. 2; EAA32833). 
CONFLICT   910   910        M -> E (in Ref. 2; EAA32833). 
Sequence information
Length: 982 AA [This is the length of the unprocessed precursor] Molecular weight: 108433 Da [This is the MW of the unprocessed precursor] CRC64: B7838C031B19687F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEAPALEQRQ SLHDSSERQQ RFTSLILPNG VGCSSREEPQ GSGGLLVPHN DNDIDNDLAS 

        70         80         90        100        110        120 
TRTASPTTTD FSSSSSDDNS TTLETSVNYS HSSNTNTNTS CPPSPITSSS LKPAYPLPPP 

       130        140        150        160        170        180 
STRLTTILPT DLKTPDHLIR DPRLIRLTGS HPFNVEPPLT ALFEHGFLTP QNLHYVRNHG 

       190        200        210        220        230        240 
PIPSSVATPP ATINKEEDDS LLNWEFTVEG LVEHPLKISV RELMDASKWD NVTYPVTLVC 

       250        260        270        280        290        300 
AGNRRKEQNV LRKSKGFSWG AGGLSTALWT GVGLSEILAR AKPLTKKGGG ARYVCFEGAD 

       310        320        330        340        350        360 
QLPNGTYGTS VKLAWAMDPN KGIMVAHKMN GENLHPDHGR PVRVVVPGQI GGRSVKWLKR 

       370        380        390        400        410        420 
IVVTKGPSEN WYHVFDNRVL PTTVGPEESG EKTEEMERVW RDERYAIYDL NVNSVICEPG 

       430        440        450        460        470        480 
HGEVVSLRGD EGAGTYRLRG YAYAGGGRRV TRLEVTLDQG KSWRLAGIEY PEDRYREAQD 

       490        500        510        520        530        540 
GEELFGGRLD VSWRESCFCW CFWDLEIPLS ELRKAKDVCI RAMDESLALQ PKEMYWSVLG 

       550        560        570        580        590        600 
MMNNPWFRVV IHHEGDTLRF EHPTQPMLTS DGWMDRVKKE GGNLANGFWG EKVPGAEENV 

       610        620        630        640        650        660 
VKEEPVKEIS MVDEKVTRLI TLEELRQHDG EEEPWFVVNG QVYNGTPFLE GHPGGAASIT 

       670        680        690        700        710        720 
GAAGQDVTDE FLAIHSENAK AMMPTYHIGT LTPSAPAALK SSSTSDPALS DPSRPIFLQS 

       730        740        750        760        770        780 
KTWNSAILTF KESVSPDTKI FHFALSHPAQ SIGLPVGQHL MMRLPDPAKP TESIIRAYTP 

       790        800        810        820        830        840 
ISDGTLERGT LRVLVKIYYA SPTEDIKGGQ MTQALDALAL GKAVEFKGPV GKFVYQGRGV 

       850        860        870        880        890        900 
CSVNGRERKV KRFVMVCGGS GVTPIYQVAE AVAVDDQDGT ECLVLDGNRV EGDILMKSEL 

       910        920        930        940        950        960 
DELVERAKPM GRCRVKYTLS RPGAEWEGLR GRLDKTMLER EVGEGDLRGE TMVLLCGPEG 

       970        980 
MQNMVREVLK GMGWKDEDVL VF 

P08619 in FASTA format

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