ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P27783

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name NIA_BETVE
Primary accession number P27783
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 62)
Name and origin of the protein
Protein name Nitrate reductase [NAD(P)H]
Synonyms NR
EC 1.7.1.2
Gene name
Name: NIA1
From
Betula verrucosa (White birch) (Betula pendula) [TaxID: 3505] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids I; Fagales; Betulaceae; Betula.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Leaf;
DOI=10.1007/BF00260713; PubMed=1675424 [NCBI, ExPASy, EBI, Israel, Japan]
Friemann A., Brinkmann K., Hachtel W.;
"Sequence of a cDNA encoding the bi-specific NAD(P)H-nitrate reductase from the tree Betula pendula and identification of conserved protein regions.";
Mol. Gen. Genet. 227:97-105(1991).
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
X54097; CAA38031.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S15959; RDBJNH.
3D structure databases
HSSP P17571; 2CND. [HSSP ENTRY / PDB]
ModBase P27783.
Ontologies
GO
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (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 InterPro).
GO:0030151; Molecular function: molybdenum ion binding (inferred from electronic annotation from InterPro).
GO:0050463; Molecular function: nitrate reductase [NAD(P)H] activity (inferred from electronic annotation from EC).
GO:0042128; Biological process: nitrate assimilation (inferred from electronic annotation from InterPro).
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.
IPR001709; FPN_cyt_redctse.
IPR005066; MoCF_OxRdtse_dimer.
IPR008335; Mopterin_OxRdtase_euk.
IPR012137; Nitr_rd_NADH.
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.
PIRSF PIRSF000233; Nitr_rd_NADH; 1.
PRINTS PR00406; CYTB5RDTASE.
PR00363; CYTOCHROMEB5.
PR00407; EUMOPTERIN.
PR00371; FPNCR.
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).
BLOCKS P27783.
ProtoNet P27783.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NAD; NADP; Nitrate assimilation; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   898  898     Nitrate reductase [NAD(P)H]. PRO_0000166075
DOMAIN   528   603  76     Cytochrome b5 heme-binding. 
DOMAIN   642   754  113     FAD-binding FR-type. 
METAL   180   180        Molybdenum-pterin (Potential). 
METAL   234   234        Molybdenum-pterin (Potential). 
METAL   563   563        Iron (heme axial ligand) (By similarity). 
METAL   586   586        Iron (heme axial ligand) (By similarity). 
DISULFID   419   419        Interchain (Potential). 
Sequence information
Length: 898 AA [This is the length of the unprocessed precursor] Molecular weight: 101002 Da [This is the MW of the unprocessed precursor] CRC64: C6B2B2B12FBCDC58 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAASVENRRF THHEPAVNGL VRTFKPVPNS HRSDSPDLGR QIPSSPKKQV ATGEDSSSED 

        70         80         90        100        110        120 
ENENDYKELI QKGNGELEPS ILDPRDEATA DNWVERNATM VRLTGKHPFN SEAPLTRLMH 

       130        140        150        160        170        180 
HGFITPAPLH YVRNHGPVPK ARWEDWSVEV CGLVKRPARF TMDRLVTEFR SREFPVTLVC 

       190        200        210        220        230        240 
AGNRRKEQNM VKKTIGFNWG AAGVSTSVWR GVPLRDVLKR CGIFSRGRGA FNVCFEGAED 

       250        260        270        280        290        300 
LPGGGGSKYG TSVKYEMAMD PARDIILGYM QNGERLSPDH GFPVRMIIPG FIGGRMVKWL 

       310        320        330        340        350        360 
KRIIVTTKES DNYYHYNDNR VLPSHVDADV AKAEAWWYKP EHIINELNIN SVITTPCHEE 

       370        380        390        400        410        420 
ILPINSWTTQ RPYTLRGYAY SGGGRKVTRV EITMNGGEKW RVCALDHPEK PNKYGKYWCW 

       430        440        450        460        470        480 
CFWSLEVEVL DLLGAKEIAV RAWDEAHNTQ PEKLIWNVMG MMNNCWFRVK TNVCKAHMGE 

       490        500        510        520        530        540 
IGIAFEHPTV PGNESGGWMA REKNLETSSD ANQSLKKSVS SPFMNTSSKM FSMSEVKKHN 

       550        560        570        580        590        600 
SAESAWIIVH GHIYDCTHFL KDHPGGADSI LINAGTDCTE EFDAIHSDKA KKMLEDYRIG 

       610        620        630        640        650        660 
ELITTGYVSD SPNSTVHGAS NTSHLAPIKE IAPLRNVALI PGAKIPTKLV YKKSLSHDVR 

       670        680        690        700        710        720 
LFRLALPSDD QVLGLPVGKH VFLCATIDDK LCMRAYTPTS TIDEVGYLDL VVKIYFKNSN 

       730        740        750        760        770        780 
PRFPNGGLMS QHLDSLPIGS VLHVKGPLGH VEYTGRGNFL VHGEPKFAKR LAMVAGGTGI 

       790        800        810        820        830        840 
TPIYQVIQAI LKDPEDETEM FVVYANRTED DILLREELDD WAKKHEKLKV WYVVKESKRE 

       850        860        870        880        890 
GWEYSVGYIR ESILREHIPE GSDDVLALAC GAPSMIEEAV RLNLEKMNYD TKNSLIIF
P27783 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by au flag APAF Australia Mirror sites: Brazil Canada China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!