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Protein

Nitrate reductase

Gene

nasA

Organism
Klebsiella oxytoca
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

Nitrite + acceptor = nitrate + reduced acceptor.

Cofactori

Protein has several cofactor binding sites:

Pathway: nitrate reduction (denitrification)

This protein is involved in step 1 of the subpathway that synthesizes dinitrogen from nitrate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Nitrate reductase (nasA)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
This subpathway is part of the pathway nitrate reduction (denitrification), which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes dinitrogen from nitrate, the pathway nitrate reduction (denitrification) and in Nitrogen metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation
Metal bindingi11 – 111Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation
Metal bindingi15 – 151Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation
Metal bindingi43 – 431Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrate assimilation

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13446.
RETL1328306-WGS:GSTH-1824-MONOMER.
UniPathwayiUPA00652; UER00706.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrate reductase (EC:1.7.99.4)
Gene namesi
Name:nasA
OrganismiKlebsiella oxytoca
Taxonomic identifieri571 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 866866Nitrate reductasePRO_0000063235Add
BLAST

Expressioni

Inductioni

By nitrate or nitrite during nitrogen-limited growth.

Interactioni

Protein-protein interaction databases

STRINGi1006551.KOX_23105.

Structurei

3D structure databases

ProteinModelPortaliQ06457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 57574Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Family and domain databases

InterProiIPR009010. 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]
PfamiPF04324. Fer2_BFD. 1 hit.
PF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTiSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06457-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTETRTTCPY CGVGCGVIAS RAPHGQVSVR GDEQHPANFG RLCVKGAALG
60 70 80 90 100
ETVGLEGRML FPEVDGERAT WPQALAAAGS RLREIIDRHG PQAVAFYASG
110 120 130 140 150
QLLTEDYYAA NKLMKGFIGA ANIDTNSRLC MSSAVTGYKR ALGADVVPCS
160 170 180 190 200
YEDVENSDLV VLVGSNAAWA HPVLYQRLAQ AKRDNPQMRV VVIDPRRTAT
210 220 230 240 250
CDIADRHLAL APGSDGGLFV GLLNAIAASG AISDDFNDAQ RALTIAQDWD
260 270 280 290 300
LDKVAQFCGL PRQQIADFYR EFIAAPRAIT LYTMGINQSA SGSDKCNAII
310 320 330 340 350
NVHLACGKYG RPGCGPFSLT GQPNAMGGRE VGGLATMLAA HMNFEPDDLR
360 370 380 390 400
RLARFWGSER LAQTPGLTGV ELFAAIGRGE VKAVWIMGTN PVVSLPDSHA
410 420 430 440 450
VSEALARCPL VIISDVVADT DTGRFAHIRF PALAWGEKSG TVTNSERRIS
460 470 480 490 500
RQRAFMPPPG EARADWWIVA RVAEALGFGS AFAWQHPHEV FSEHAALSGY
510 520 530 540 550
ENDGQRAFDI GGLADLSREA WDALEPVRWP VSRSEAAWSV HKGWHRDGKL
560 570 580 590 600
RMVPVAPQPT RATTDAFYPL ILNSGRIRDQ WHTMTRTGAV PRLMQHINEP
610 620 630 640 650
VVEVAPADAQ RYHLLEGELA RVRSPKGVMV AKVTIGDGQR PGSLFVPMHW
660 670 680 690 700
NNQFARQGRV NNLLAAVTDP HSGQPESKQT AVAIATWLPA WKGELFSRQP
710 720 730 740 750
VPLPASLHWR RRAAQGIIHL SLAGDTRSRD WLVEWCQRQG WQMQVAEGGK
760 770 780 790 800
VWNLLAWRAG ELMLGWWSDA SEPAIDADWI HAAFRVPPQN AARRHALLSG
810 820 830 840 850
RKGGVEMPRG RIICSCFSVG ERAIGEAIAG GCRTPGALGG KLKCGTNCGS
860
CIPELKALLA AKLAQA
Length:866
Mass (Da):93,897
Last modified:August 14, 2001 - v2
Checksum:i2B6B464578784DD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06800 Genomic DNA. Translation: AAA25100.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06800 Genomic DNA. Translation: AAA25100.2.

3D structure databases

ProteinModelPortaliQ06457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1006551.KOX_23105.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00652; UER00706.
BioCyciMetaCyc:MONOMER-13446.
RETL1328306-WGS:GSTH-1824-MONOMER.

Family and domain databases

InterProiIPR009010. 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]
PfamiPF04324. Fer2_BFD. 1 hit.
PF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTiSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiNASA_KLEOX
AccessioniPrimary (citable) accession number: Q06457
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: August 14, 2001
Last modified: June 24, 2015
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.