Periplasmic nitrate reductase precursor - Escherichia coli O45:K1 (strain S88 / ExPEC)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Periplasmic nitrate reductase
EC=1.7.99.4

Gene names

Name:	napA
Ordered Locus Names:	ECS88_2353

Organism

Escherichia coli O45:K1 (strain S88 / ExPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

585035 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	828 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein NapC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism By similarity. HAMAP-Rule MF_01630
Catalytic activity	Nitrite + acceptor = nitrate + reduced acceptor. HAMAP-Rule MF_01630
Cofactor	Binds 1 4Fe-4S cluster By similarity. Binds 1 molybdenum ion per subunit By similarity. Binds 2 molybdopterin guanine dinucleotide (MGD) groups per subunit By similarity.
Subunit structure	Interacts with NapB By similarity.
Subcellular location	Periplasm By similarity.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. HAMAP-Rule MF_01630
Sequence similarities	Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.

Ontologies

Keywords
Biological process	Electron transport Nitrate assimilation Transport
Cellular component	Periplasm
Domain	Signal
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Molybdenum
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: HAMAP electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrate assimilation Inferred from electronic annotation. Source: HAMAP
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: HAMAP iron ion binding Inferred from electronic annotation. Source: HAMAP molybdenum ion binding Inferred from electronic annotation. Source: InterPro nitrate reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Tat-type signal Potential

Chain

32 – 828

797

Periplasmic nitrate reductase HAMAP-Rule MF_01630

PRO_1000186354

Sites

Metal binding

46

1

Iron-sulfur (4Fe-4S) By similarity

Metal binding

49

1

Iron-sulfur (4Fe-4S) By similarity

Metal binding

53

1

Iron-sulfur (4Fe-4S) By similarity

Metal binding

81

1

Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

B7MFB8 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 0DEEBF668E60A1DB
Show »

FASTA

828

93,058

        10         20         30         40         50         60 
MKLSRRSFMK ANAVAAAAAA AGLSVPGVAR AVVGQQEAIK WDKAPCRFCG TGCGVLVGTQ 

        70         80         90        100        110        120 
QGRVVACQGD PDAPVNRGLN CIKGYFLPKI MYGKDRLTQP LLRMKNGKYD KEGEFTPITW 

       130        140        150        160        170        180 
DQAFDVMEDK FKTALKEKGP ESIGMFGSGQ WTIWEGYAAS KLFKAGFRSN NIDPNARHCM 

       190        200        210        220        230        240 
ASAVVGFMRT FGMDEPMGCY DDIEQADAFV LWGSNMAEMH PILWSRITNR RLSNQNVTVA 

       250        260        270        280        290        300 
VLSTYQHRSF ELADNGIIFT PQSDLVILNY IANYIIQNNA INQDFFSKHV NLRKGATDIG 

       310        320        330        340        350        360 
YGLRPTHPLE KAAKNPGSDA SEPMSFEDYK AFVAEYTLEK TAEMTGVPKD QLEQLAQLYA 

       370        380        390        400        410        420 
DPNKKVISYW TMGFNQHTRG VWANNLVYNL HLLTGKISQP GCGPFSLTGQ PSACGTAREV 

       430        440        450        460        470        480 
GTFAHRLPAD MVVTNEKHRD ICEKKWNIPS GTIPAKIGLH AVAQDRALKD GKLNVYWTMC 

       490        500        510        520        530        540 
TNNMQAGPNI NEERMPGWRD PRNFIIVSDP YPTVSALAAD LILPTAMWVE KEGAYGNAER 

       550        560        570        580        590        600 
RTQFWRQQVQ APGEAKSDLW QLVQFSRRFK TEEVWPEELL AKKPELRGKT LYEVLYATPE 

       610        620        630        640        650        660 
VSKFPVSELA EDQLNDESRE LGFYLQKGLF EEYAWFGRGH GHDLAPFDDY HKARGLRWPV 

       670        680        690        700        710        720 
VNGKETQWRY SEGNDPYVKA GEGYKFYGKP DGKAVIFALP FEPAAEAPDE EYDLWLSTGR 

       730        740        750        760        770        780 
VLEHWHTGSM TRRVPELHRA FPEAVLFIHP LDAKARDLRR GDKVKVVSRR GEVISIVETR 

       790        800        810        820 
GRNRPPQGLV YMPFFDAAQL VNKLTLDATD PLSKETDFKK CAVKLEKV

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References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths."
Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.

Denamur E.
PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S88 / ExPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928161 Genomic DNA. Translation: CAR03634.1.
RefSeq	YP_002392036.1. NC_011742.1.
3D structure databases
ProteinModelPortal	B7MFB8.
SMR	B7MFB8. Positions 1-35, 37-827.
ModBase	Search...
Protein-protein interaction databases
STRING	585035.ECS88_2353.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAR03634; CAR03634; ECS88_2353.
GeneID	7129672.
KEGG	ecz:ECS88_2353.
PATRIC	18412420. VBIEscCol91599_2333.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0243.
HOGENOM	HOG000031441.
KO	K02567.
OMA	HWIKAAR.
ProtClustDB	PRK13532.
Enzyme and pathway databases
BioCyc	ECOL585035:GJWP-2345-MONOMER.
Family and domain databases
Gene3D	2.40.40.20. 1 hit.
HAMAP	MF_01630. Nitrate_reduct.
InterPro	IPR009010. Asp_de-COase-like_dom. IPR006657. MoPterin_dinucl-bd_dom. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4_dom. IPR006655. Mopterin_OxRdtase_prok_CS. IPR010051. Periplasm_NO3_reductase_lsu. IPR006311. TAT_signal. IPR019546. TAT_signal_bac_arc. [Graphical view]
Pfam	PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. [Graphical view]
SMART	SM00926. Molybdop_Fe4S4. 1 hit. [Graphical view]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMs	TIGR01706. NAPA. 1 hit. TIGR01409. TAT_signal_seq. 1 hit.
PROSITE	PS00551. MOLYBDOPTERIN_PROK_1. 1 hit. PS00490. MOLYBDOPTERIN_PROK_2. False negative. PS00932. MOLYBDOPTERIN_PROK_3. False negative. PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAPA_ECO45

Accession

Primary (citable) accession number: B7MFB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents