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Q06457 (NASA_KLEOX) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nitrate reductase

EC=1.7.99.4
Gene names
Name:nasA
OrganismKlebsiella oxytoca
Taxonomic identifier571 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length866 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.

Catalytic activity

Nitrite + acceptor = nitrate + reduced acceptor.

Cofactor

Binds 1 4Fe-4S cluster Potential.

Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit By similarity.

Pathway

Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 1/4.

Induction

By nitrate or nitrite during nitrogen-limited growth.

Sequence similarities

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 866866Nitrate reductase
PRO_0000063235

Regions

Domain1 – 57574Fe-4S Mo/W bis-MGD-type

Sites

Metal binding81Iron-sulfur (4Fe-4S) By similarity
Metal binding111Iron-sulfur (4Fe-4S) By similarity
Metal binding151Iron-sulfur (4Fe-4S) By similarity
Metal binding431Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q06457 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: 2B6B464578784DD5

FASTA86693,897
        10         20         30         40         50         60 
MTETRTTCPY CGVGCGVIAS RAPHGQVSVR GDEQHPANFG RLCVKGAALG ETVGLEGRML 

        70         80         90        100        110        120 
FPEVDGERAT WPQALAAAGS RLREIIDRHG PQAVAFYASG QLLTEDYYAA NKLMKGFIGA 

       130        140        150        160        170        180 
ANIDTNSRLC MSSAVTGYKR ALGADVVPCS YEDVENSDLV VLVGSNAAWA HPVLYQRLAQ 

       190        200        210        220        230        240 
AKRDNPQMRV VVIDPRRTAT CDIADRHLAL APGSDGGLFV GLLNAIAASG AISDDFNDAQ 

       250        260        270        280        290        300 
RALTIAQDWD LDKVAQFCGL PRQQIADFYR EFIAAPRAIT LYTMGINQSA SGSDKCNAII 

       310        320        330        340        350        360 
NVHLACGKYG RPGCGPFSLT GQPNAMGGRE VGGLATMLAA HMNFEPDDLR RLARFWGSER 

       370        380        390        400        410        420 
LAQTPGLTGV ELFAAIGRGE VKAVWIMGTN PVVSLPDSHA VSEALARCPL VIISDVVADT 

       430        440        450        460        470        480 
DTGRFAHIRF PALAWGEKSG TVTNSERRIS RQRAFMPPPG EARADWWIVA RVAEALGFGS 

       490        500        510        520        530        540 
AFAWQHPHEV FSEHAALSGY ENDGQRAFDI GGLADLSREA WDALEPVRWP VSRSEAAWSV 

       550        560        570        580        590        600 
HKGWHRDGKL RMVPVAPQPT RATTDAFYPL ILNSGRIRDQ WHTMTRTGAV PRLMQHINEP 

       610        620        630        640        650        660 
VVEVAPADAQ RYHLLEGELA RVRSPKGVMV AKVTIGDGQR PGSLFVPMHW NNQFARQGRV 

       670        680        690        700        710        720 
NNLLAAVTDP HSGQPESKQT AVAIATWLPA WKGELFSRQP VPLPASLHWR RRAAQGIIHL 

       730        740        750        760        770        780 
SLAGDTRSRD WLVEWCQRQG WQMQVAEGGK VWNLLAWRAG ELMLGWWSDA SEPAIDADWI 

       790        800        810        820        830        840 
HAAFRVPPQN AARRHALLSG RKGGVEMPRG RIICSCFSVG ERAIGEAIAG GCRTPGALGG 

       850        860 
KLKCGTNCGS CIPELKALLA AKLAQA 

« Hide

References

[1]"Structures of genes nasA and nasB, encoding assimilatory nitrate and nitrite reductases in Klebsiella pneumoniae M5al."
Lin J.T., Goldman B.S., Stewart V.
J. Bacteriol. 175:2370-2378(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: M5a1.
[2]Stewart V.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06800 Genomic DNA. Translation: AAA25100.2.

3D structure databases

ProteinModelPortalQ06457.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13446.
RETL1328306-WGS:GSTH-1824-MONOMER.
UniPathwayUPA00652; UER00706.

Family and domain databases

InterProIPR009010. Asp_de-COase-like_dom.
IPR007419. BFD-like_2Fe2S-bd_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR027467. MopterinOxRdtase_cofactor_BS.
[Graphical view]
PfamPF04324. Fer2_BFD. 1 hit.
PF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMSSF50692. SSF50692. 1 hit.
PROSITEPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNASA_KLEOX
AccessionPrimary (citable) accession number: Q06457
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: August 14, 2001
Last modified: July 9, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways