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UniProtKB/Swiss-Prot entry P49050


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

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Entry information
Entry name NIA_PICAN
Primary accession number P49050
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on February 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 65)
Name and origin of the protein
Protein name Nitrate reductase [NADPH]
Synonyms NR
EC 1.7.1.3
Gene name
Name: YNR1
From
Pichia angusta (Yeast) (Hansenula polymorpha) [TaxID: 4905] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Pichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 14754 / IFO 0799 / JCM 3620 / NCYC 495 / NRRL Y-1798;
DOI=10.1016/0014-5793(95)00511-7; PubMed=7789531 [NCBI, ExPASy, EBI, Israel, Japan]
Avila J., Perez M.D., Brito N., Gonzalez C., Siverio J.M.;
"Cloning and disruption of the YNR1 gene encoding the nitrate reductase apoenzyme of the yeast Hansenula polymorpha.";
FEBS Lett. 366:137-142(1995).
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
Z49110; CAA88925.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S65938; S65938.
3D structure databases
PDB
2BIH; X-ray; 2.60 A; A=19-478.[ExPASy / RCSB / EBI]
2BII; X-ray; 1.70 A; A/B=59-478.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2BIH; -.
2BII; -.
ModBase P49050.
Ontologies
GO
GO:0050464; Molecular function: nitrate reductase (NADPH) activity (inferred from electronic annotation from EC).
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 P49050.
Other
ProtoNet P49050.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; 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   859  859     Nitrate reductase [NADPH]. PRO_0000166044
DOMAIN   502   578  77     Cytochrome b5 heme-binding. 
DOMAIN   602   713  112     FAD-binding FR-type. 
NP_BIND   829   838  10     NADP (By similarity). 
METAL   137   137        Molybdenum-pterin (Potential). 
METAL   538   538        Iron (heme axial ligand) (By similarity). 
METAL   561   561        Iron (heme axial ligand) (By similarity). 
DISULFID   383   383        Interchain (Potential). 
HELIX   38    41  4      
TURN   44    47  4      
STRAND   63    65  3      
HELIX   69    74  6      
HELIX   81    83  3      
STRAND   86    90  5      
HELIX   97   102  6      
STRAND   104   113  10      
STRAND   115   118  4      
HELIX   119   125  7      
STRAND   129   136  8      
TURN   138   141  4      
HELIX   142   148  7      
STRAND   161   170  10      
HELIX   171   178  8      
STRAND   186   192  7      
STRAND   201   205  5      
HELIX   206   209  4      
TURN   212   214  3      
STRAND   217   222  6      
HELIX   229   231  3      
TURN   232   234  3      
STRAND   236   238  3      
HELIX   244   246  3      
STRAND   249   259  11      
HELIX   264   267  4      
STRAND   268   271  4      
HELIX   279   284  6      
HELIX   286   289  4      
HELIX   292   294  3      
STRAND   302   308  7      
STRAND   313   315  3      
STRAND   320   328  9      
STRAND   335   343  9      
STRAND   352   354  3      
HELIX   357   362  6      
STRAND   365   368  4      
STRAND   371   373  3      
HELIX   375   377  3      
STRAND   385   392  8      
HELIX   393   397  5      
STRAND   400   408  9      
STRAND   431   438  8      
STRAND   441   445  5      
HELIX   456   462  7      
TURN   470   473  4      
Sequence information
Length: 859 AA [This is the length of the unprocessed precursor] Molecular weight: 98534 Da [This is the MW of the unprocessed precursor] CRC64: 79569977B01E3967 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDSIVTEVTY GLEIKKIKDI TELPFPVRQD SPLTEVLPTD LKTKDNFVAR DPDLLRLTGS 

        70         80         90        100        110        120 
HPFNSEPPLT KLYDSGFLTP VSLHFVRNHG PVPYVPDENI LDWEVSIEGM VETPYKIKLS 

       130        140        150        160        170        180 
DIMEQFDIYS TPVTMVCAGN RRKEQNMVKK GAGFNWGAAG TSTSLWTGCM LGDVIGKARP 

       190        200        210        220        230        240 
SKRARFVWME GADNPANGAY RTCIRLSWCM DPERCIMIAY QQNGEWLHPD HGKPLRVVIP 

       250        260        270        280        290        300 
GVIGGRSVKW LKKLVVSDRP SENWYHYFDN RVLPTMVTPE MAKSDDRWWK DERYAIYDLN 

       310        320        330        340        350        360 
LQTIICKPEN QQVIKISEDE YEIAGFGYNG GGVRIGRIEV SLDKGKSWKL ADIDYPEDRY 

       370        380        390        400        410        420 
REAGYFRLFG GLVNVCDRMS CLCWCFWKLK VPLSELARSK DILIRGMDER MMVQPRTMYW 

       430        440        450        460        470        480 
NVTSMLNNWW YRVAIIREGE SLRFEHPVVA NKPGGWMDRV KAEGGDILDN NWGEVDDTVK 

       490        500        510        520        530        540 
QAERRPHIDE DLEMMCNREK MDVVIKYSEF EAHKDSETEP WFAVKGQVFD GSSYLEDHPG 

       550        560        570        580        590        600 
GAQSILMVSG EDATDDFIAI HSSFAKKLLP SMHLGRLEEV SSVTKVKSVE QNVKREVLLD 

       610        620        630        640        650        660 
PRKWHKITLA EKEVISSDSR IFKFDLEHSE QLSGLPTGKH LFLRLKDSSG KYVMRAYTPK 

       670        680        690        700        710        720 
SSNSLRGRLE ILIKVYFPNR EYPNGGIMTN LIENLQVGNQ IEVKGPVGEF EYVKCGHCSF 

       730        740        750        760        770        780 
NNKPYQMKHF VMISGGSGIT PTYQVLQAIF SDPEDRTSVQ LFFGNKKVDD ILLREELDHI 

       790        800        810        820        830        840 
QEKYPEQFKV DYSLSDLDHL PENWSGVRGR LTFDILDTYV RGKKMGEYML LVCGPPGMNG 

       850 
VVENWCNARK LDKQYVVYF 

P49050 in FASTA format

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View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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