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UniProtKB/Swiss-Prot entry P17570

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

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Entry information
Entry name NIA_SOLLC
Primary accession number P17570
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on August 1, 1990 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 74)
Name and origin of the protein
Protein name Nitrate reductase [NADH]
Synonyms NR
EC 1.7.1.1
Gene name
Name: NIA
From
Solanum lycopersicum (Tomato) (Lycopersicon esculentum) [TaxID: 4081] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum; Lycopersicon.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Manapal;
TISSUE=Leaf;
DOI=10.1016/0378-1119(89)90430-7; PubMed=2628174 [NCBI, ExPASy, EBI, Israel, Japan]
Daniel-Vedele F., Dorbe M.F., Caboche M., Rouze P.;
"Cloning and analysis of the tomato nitrate reductase-encoding gene: protein domain structure and amino acid homologies in higher plants.";
Gene 85:371-380(1989).
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
X14060; CAA32218.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JQ0373; RDTONH.
3D structure databases
HSSP P17571; 2CND. [HSSP ENTRY / PDB]
ModBase P17570.
Ontologies
GO
GO:0009703; Molecular function: nitrate reductase (NADH) activity (inferred from electronic annotation from EC).
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 P17570.
ProtoNet P17570.
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   911  911     Nitrate reductase [NADH]. PRO_0000166061
DOMAIN   536   611  76     Cytochrome b5 heme-binding. 
DOMAIN   654   766  113     FAD-binding FR-type. 
METAL   188   188        Molybdenum-pterin (Potential). 
METAL   242   242        Molybdenum-pterin (Potential). 
METAL   571   571        Iron (heme axial ligand) (By similarity). 
METAL   594   594        Iron (heme axial ligand) (By similarity). 
DISULFID   427   427        Interchain (Potential). 
Sequence information
Length: 911 AA [This is the length of the unprocessed precursor] Molecular weight: 102453 Da [This is the MW of the unprocessed precursor] CRC64: DE8736181F02A0D5 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAASVENRQY THLEPGLSGV GRTFKPRPDS PVRGCNFPPS SNHELPFQKK QNPPIYLDYS 

        70         80         90        100        110        120 
SSEDEDDDDE KNEYVQMIKK GKTELEPSIH DTRDEGTADN WIERNFSLIR LTGKHPFNSE 

       130        140        150        160        170        180 
PPLSRLMHHG FITPVPLHYV RNHGPVPKAS WSDWTVEVTG LVKRPMKFTM DQLVNEFPSR 

       190        200        210        220        230        240 
EFPVTLVCAG NRRKEQNMVK QTIGFNWGAA AVSTTVWRGV PLRALLKRCG VQSKKKGALN 

       250        260        270        280        290        300 
VCFEGSDVLP GGGGSKYGTS IKKEFAMDPS RDIIVAYMQN GEMLSPDHGF PVRMIIPGFI 

       310        320        330        340        350        360 
GGRMVKWLKR IVVTTQESES YYHYKDNRVL PPHVDAELAN AEAWWYKPEY IINELNINSV 

       370        380        390        400        410        420 
ITTPCHEEIL PINAWTTQRP YTLRGYAYSG GGKKVTRVEV TLDGGETWSV CTLDHPEKPT 

       430        440        450        460        470        480 
KYGKYWCWCF WSLEVEVLDL LSAKEIAVRA TDETLNTQPE KLIWNVMGMM NNCWFRVKMN 

       490        500        510        520        530        540 
VCKPHKGEIG IVFEHPTQPG NQSGGWMAKE RHLEISAVAP PTLKKSISTP FMNTASKMYS 

       550        560        570        580        590        600 
MSEVRKHNSS DSAWIIVHGH IYDASRFLKD HPGGVDSILI NAGTDCTEEF DAIHSDKAKK 

       610        620        630        640        650        660 
LLEDFRIGEL ITTGYTSDSS PNSSVHGSSS ISSFLAPIKE LVQTPTRSVA LIPREKIPCK 

       670        680        690        700        710        720 
LVDKQSISHD VRKFKFALPS EDQVLGLPVG KHIFLCATVD DKLCMRAYTP TSTVDEVGFF 

       730        740        750        760        770        780 
ELVVKIYFKG VHPKFPNGGQ MSQHLDSLPI GAFLDVKGPL GHIEYQGKGN FLVHGKQKFA 

       790        800        810        820        830        840 
KKLAMIAGGT GITPVYQVMQ SILKDPEDDT EMYVVYANRT EDDILLKDEL DAWAEQVPNR 

       850        860        870        880        890        900 
VKVWYVVQES ITQGWKYSTG FVTESILREH IPEPSHTTLA LACGPPPMIQ FAINPNLEKM 

       910 
GYDIKEELLV F
P17570 in FASTA format

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