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 P27967


[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 NIA1_HORVU
Primary accession number P27967
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 64)
Name and origin of the protein
Protein name Nitrate reductase [NADH]
Synonyms NR
EC 1.7.1.1
Gene name None
From
Hordeum vulgare (Barley) [TaxID: 4513] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; Pooideae; Triticeae; Hordeum.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Himalaya;
TISSUE=Leaf;
DOI=10.1007/BF00273931; PubMed=1865878 [NCBI, ExPASy, EBI, Israel, Japan]
Schnorr K.M., Juricek M., Huang C., Culley D., Kleinhofs A.;
"Analysis of barley nitrate reductase cDNA and genomic clones.";
Mol. Gen. Genet. 227:411-416(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
X57845; CAA40976.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S17453; RDBHNH.
3D structure databases
HSSP P17571; 2CND. [HSSP ENTRY / PDB]
SMR P27967; 656-915.
ModBase P27967.
Organism-specific databases
Gramene P27967; -.
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:0009703; Molecular function: nitrate reductase (NADH) 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).
ProtoNet P27967.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NAD; Nitrate assimilation; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   915  915     Nitrate reductase [NADH]. PRO_0000166056
DOMAIN   538   613  76     Cytochrome b5 heme-binding. 
DOMAIN   654   767  114     FAD-binding FR-type. 
METAL   189   189        Molybdenum-pterin (Potential). 
METAL   243   243        Molybdenum-pterin (Potential). 
METAL   573   573        Iron (heme axial ligand) (By similarity). 
METAL   596   596        Iron (heme axial ligand) (By similarity). 
DISULFID   428   428        Interchain (Potential). 
Sequence information
Length: 915 AA [This is the length of the unprocessed precursor] Molecular weight: 101770 Da [This is the MW of the unprocessed precursor] CRC64: 937FFA96B6FDAA56 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAASVEPRQP FGRLDAPATA PTARAPGSNG IRRRADSPVR GCGFPSLISP PRKGPVAEEE 

        70         80         90        100        110        120 
EDDDDEDDEG HEDWREAYGS HLQLEVEPST RDPRDEGTAD AWIERNPSLI RLTGKHPLNC 

       130        140        150        160        170        180 
EPPLARLMHH GFITPAPLHY VRNHGAVPRG DWATWTVEVT GLVRRPARLT MDELANGFPA 

       190        200        210        220        230        240 
AEVPATLVCA GNRRKEQNMV QQTVGFNWGA AGVSTSVWRG ARLRDVLLRC GVMSKKGQAL 

       250        260        270        280        290        300 
NVCFEGAEDL PGGGGSKYGT SVSREWAMDP SRDIILPYAQ NGEPLLPDHG YPVRVLIPGC 

       310        320        330        340        350        360 
IGGRMVKWVR RIVVTTAESD NYYHFKDNRV LPSHVDAELA NAEAWWYRPE YIINELNTNC 

       370        380        390        400        410        420 
VITTPGHDEI LPINAFTTQR AYTIKGYAYS GGGKKITRVE VTLDGGESWM LCTLDIPEKP 

       430        440        450        460        470        480 
NKYGRYWCWC FWSVEIEVLD LLGAKEVAVR TWDQTHNTQP EKLIWNLMGM MNNCWFKIKV 

       490        500        510        520        530        540 
NVCRPHKGEI GLVFEHPTQP GNQTGGWMAR QKHLETAEAA APGLKRSTST PFMNTAGDKQ 

       550        560        570        580        590        600 
FTMSEVRKHG SKESAWIVVH GHVYDCTAFL KDHPGGADSI LINAGSDCTE EFDAIHSDKA 

       610        620        630        640        650        660 
KALLDTYRIG ELITTGTGYN SDNSVHGGSS LSHLAPIREA TKVAGAPIAL SSPREKVPCR 

       670        680        690        700        710        720 
LVDKKELSHD VRLFRFALPS SDQVLGLPVG KHIFVCATID GKLCMRAYTP TSMVDEIGQF 

       730        740        750        760        770        780 
ELLVKVYFRD EHPKFPNGGL MTQYLESLQV GSSYIDVKGP LGHVEYTGRG NFVINGKQRR 

       790        800        810        820        830        840 
ARRLAMICGG SGITPMYQVI QAVLRDQPED ETEMHLVYAN RSEDDILLRD ELDRWAAEYP 

       850        860        870        880        890        900 
DRLKVWYVID QVKRPEDGWK FSVGFVTEDI LRAHVPEGGD DTLALACGPP PMIKFAISPN 

       910 
LEKMKYDMAN SFISF 

P27967 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 ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!