Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q53176 (NAPA_RHOS4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 111. 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:
Periplasmic nitrate reductase

EC=1.7.99.4
Gene names
Name:napA
Ordered Locus Names:RHOS4_40230
ORF Names:RSP_4116
Encoded onPlasmid pRS241c Ref.2
OrganismRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [Reference proteome] [HAMAP]
Taxonomic identifier272943 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length831 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. HAMAP-Rule MF_01630

Catalytic activity

Nitrite + acceptor = nitrate + reduced acceptor. HAMAP-Rule MF_01630

Cofactor

Binds 1 4Fe-4S cluster By similarity. HAMAP-Rule MF_01630

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

Subunit structure

Interacts with NapB.

Subcellular location

Periplasm HAMAP-Rule MF_01630.

Induction

Nitrate reductase activity can be induced by nitrate and not repressed by ammonium or oxygen. HAMAP-Rule MF_01630

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.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929Tat-type signal Potential
Chain30 – 831802Periplasmic nitrate reductase HAMAP-Rule MF_01630
PRO_0000019171

Regions

Domain41 – 97574Fe-4S Mo/W bis-MGD-type

Sites

Metal binding481Iron-sulfur (4Fe-4S) By similarity
Metal binding511Iron-sulfur (4Fe-4S) By similarity
Metal binding551Iron-sulfur (4Fe-4S) By similarity
Metal binding831Iron-sulfur (4Fe-4S) By similarity

Experimental info

Sequence conflict1351R → L in CAA86827. Ref.1
Sequence conflict1411G → A Ref.1
Sequence conflict1431K → E Ref.1
Sequence conflict2521M → S in CAA86827. Ref.1
Sequence conflict2551A → S in CAA86827. Ref.1
Sequence conflict2671L → R in CAA86827. Ref.1
Sequence conflict3691V → W in CAA86827. Ref.1
Sequence conflict4151S → F in CAA86827. Ref.1
Sequence conflict5211C → A in CAA86827. Ref.1
Sequence conflict6601R → H in CAA86827. Ref.1
Sequence conflict7371V → W in CAA86827. Ref.1

Secondary structure

........................................................................................................................................................ 831
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q53176 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 74B35640749CC906

FASTA83192,637
        10         20         30         40         50         60 
MTLTRRDLIK AQAAATAAAA AGLPVSALAQ PVTGGAEALR IRWSKAPCRF CGTGCGVMVG 

        70         80         90        100        110        120 
TRDGQVVATH GDTQAEVNRG LNCVKGYFLS KIMYGEDRLT TPLLRMKDGV YHKEGEFAPV 

       130        140        150        160        170        180 
SWDEAFDVMA AQAKRVLKEK GPKAVGMFGS GQWTIWEGYA ASKLMRAGFR SNNLDPNARH 

       190        200        210        220        230        240 
CMASAATAFM RTFGMDEPMG CYDDFEAADA FVLWGSNMAE MHPILWSRLT DRRLSHEHVR 

       250        260        270        280        290        300 
VAVLSTFTHR SMDLADTPII FRPGTDLAIL NYIAHHIIST GRVNRDFVDR HTNFALGATD 

       310        320        330        340        350        360 
IGYGLRPEHQ LQLAAKGAAD AGAMTPTDFE TFAALVSEYT LEKAAEISGV EPALLEELAE 

       370        380        390        400        410        420 
LYADPDRKVM SLWTMGFNQH VRGVWANHMV YNLHLLTGKI SEPGNSPFSL TGQPSACGTA 

       430        440        450        460        470        480 
REVGTFAHRL PADMVVTNPE HRAHAEEIWK LPAGLLPDWV GAHAVEQDRK LHDGEINFYW 

       490        500        510        520        530        540 
VQVNNNMQAA PNIDQETYPG YRNPENFIVV SDAYPTVTGR CADLVLPAAM WVEKEGAYGN 

       550        560        570        580        590        600 
AERRTHFWHQ LVEAPGEARS DLWQLMEFSK RFTTDEVWPE EILSAAPAYR GKTLFEVLFA 

       610        620        630        640        650        660 
NGSVDRFPAS DVNPDHANHE AALFGFYPQK GLFEEYAAFG RGHGHDLAPF DTYHEVRGLR 

       670        680        690        700        710        720 
WPVVEGEETR WRYREGFDPY VKPGEGLRFY GKPDGRAVIL GVPYEPPAES PDEEFGFWLV 

       730        740        750        760        770        780 
TGRVLEHWHS GSMTLRVPEL YKAFPGAVCF MHPEDARSRG LNRGSEVRVI SRRGEIRTRL 

       790        800        810        820        830 
ETRGRNRMPR GVVFVPWFDA SQLINKVTLD ANDPISRQTD FKKCAVKIEA V 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of periplasmic nitrate reductase genes from Rhodobacter sphaeroides DSM 158: structural and functional differences among prokaryotic nitrate reductases."
Reyes F., Roldan M.D., Klipp W., Castillo F., Moreno-Vivian C.
Mol. Microbiol. 19:1307-1318(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of plasmid C of Rhodobacter sphaeroides 2.4.1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
[3]"Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase."
Arnoux P., Sabaty M., Alric J., Frangioni B., Guigliarelli B., Adriano J.-M., Pignol D.
Nat. Struct. Biol. 10:928-934(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH NAPB.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z46806 Genomic DNA. Translation: CAA86827.1.
CP000146 Genomic DNA. Translation: ABA81591.1.
RefSeqYP_345332.1. NC_007489.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OGYX-ray3.20A/C/E/G/I/K/M/O30-831[»]
ProteinModelPortalQ53176.
SMRQ53176. Positions 41-829.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ53176. 1 interaction.
STRING272943.RSP_4116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA81591; ABA81591; RSP_4116.
GeneID3711832.
KEGGrsp:RSP_4116.
PATRIC23149531. VBIRhoSph57909_0178.

Phylogenomic databases

eggNOGCOG0243.
HOGENOMHOG000031441.
KOK02567.
OMARRTHVWH.
OrthoDBEOG6CVV7G.
ProtClustDBPRK13532.

Enzyme and pathway databases

BioCycRSPH272943:GJAS-4224-MONOMER.

Family and domain databases

HAMAPMF_01630. Nitrate_reduct.
InterProIPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR027467. MopterinOxRdtase_cofactor_BS.
IPR010051. Periplasm_NO3_reductase_lsu.
IPR006311. TAT_signal.
IPR019546. TAT_signal_bac_arc.
[Graphical view]
PfamPF04879. 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.
TIGRFAMsTIGR01706. NAPA. 1 hit.
TIGR01409. TAT_signal_seq. 1 hit.
PROSITEPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ53176.

Entry information

Entry nameNAPA_RHOS4
AccessionPrimary (citable) accession number: Q53176
Secondary accession number(s): Q3IV43
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 24, 2006
Last modified: February 19, 2014
This is version 111 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references