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Protein

Periplasmic nitrate reductase

Gene

napA

Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.UniRule annotation

Catalytic activityi

2 ferrocytochrome + nitrate + 2 H+ = 2 ferricytochrome + nitrite.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster.UniRule annotation
  • Mo-bis(molybdopterin guanine dinucleotide)UniRule annotationNote: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi48Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi51Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi55Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi83Iron-sulfur (4Fe-4S)UniRule annotation1
Binding sitei85Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei152Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei177Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei181Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei375Mo-bis(molybdopterin guanine dinucleotide); via amide nitrogenUniRule annotation1
Binding sitei379Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei485Mo-bis(molybdopterin guanine dinucleotide); via amide nitrogenUniRule annotation1
Binding sitei534Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei561Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei797Substrate; via amide nitrogenUniRule annotation1
Binding sitei805Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei822Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Nitrate assimilation, Transport
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic nitrate reductaseUniRule annotation (EC:1.9.6.1UniRule annotation)
Gene namesi
Name:napAUniRule annotation
Ordered Locus Names:BPP2702
OrganismiBordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Taxonomic identifieri257311 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
Proteomesi
  • UP000001421 Componenti: Chromosome

Subcellular locationi

  • Periplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 38Tat-type signalUniRule annotationAdd BLAST38
ChainiPRO_000004597839 – 831Periplasmic nitrate reductaseUniRule annotationAdd BLAST793

Post-translational modificationi

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.UniRule annotation

Interactioni

Subunit structurei

Component of the periplasmic nitrate reductase NapAB complex composed of NapA and NapB.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ7W733.
SMRiQ7W733.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 974Fe-4S Mo/W bis-MGD-typeUniRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni214 – 221Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotation8
Regioni245 – 249Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotation5
Regioni264 – 266Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotation3
Regioni511 – 512Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotation2
Regioni721 – 730Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotation10

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000031441.
KOiK02567.
OMAiTTDEVWP.

Family and domain databases

HAMAPiMF_01630. Nitrate_reduct_NapA. 1 hit.
InterProiView protein in InterPro
IPR009010. Asp_de-COase-like_dom_sf.
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.
PANTHERiPTHR11615:SF123. PTHR11615:SF123. 1 hit.
PfamiView protein in Pfam
PF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
SMARTiView protein in SMART
SM00926. Molybdop_Fe4S4. 1 hit.
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR01706. NAPA. 1 hit.
TIGR01409. TAT_signal_seq. 1 hit.
PROSITEiView protein in PROSITE
PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS51318. TAT. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7W733-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMARRDFIK QTAAAAAATV AGVPLTGYTQ NIVTESEAAK LKWSKAPCRF
60 70 80 90 100
CGTGCGVNVA VKDNQVVATH GDFNAEVNKG LNCVKGYFLS KIMYGSDRLT
110 120 130 140 150
QPLLRIKDGK YAKDGEFAPV SWDQAFDVMA EQFKRVLKDK GPEAVGMFGS
160 170 180 190 200
GQWTVWEGYA ALKLMKAGFR TNNLDPNARH CMASAAVGFM RTFGADEPMG
210 220 230 240 250
CYDDIENADA FVLWGSNMAE MHPILWTRVT DRRLSAPATK VAVLSTFEHR
260 270 280 290 300
SYELADLTLT FEPQSDLAIL NYIANHIIRT KRVNRDFVDK HTVFREGNAD
310 320 330 340 350
IGYGLRPEHP LQQAARNAGD AGGSKPITFD DFARFVSKYD LEYTAKLSGV
360 370 380 390 400
PKNRLEELAE LYADPKVRVT SFWTMGFNQH TRGVWCNNMV YNIHLLTGKI
410 420 430 440 450
STPGNSPFSL TGQPSACGTA REVGTFSHRL PADLVVTNPE HRRHAEEIWK
460 470 480 490 500
LPDGTIPSKV GAHAVLQNRM LKDGKINAYW VMVNNNMQAA ANLMNEGLPG
510 520 530 540 550
YRNPENFIVV SDAYPTVTTL SADLILPAAM WVEKEGAYGN AERRTQFWHQ
560 570 580 590 600
LVDAPGQARS DLWQLVEFSK RFKVEEVWPA DLLAKKPEYR GKTLYDVLFA
610 620 630 640 650
NGKVNQFPNT ELDPEYANQE AQAFGFYLQK GLFEEYAEFG RGHGHDLAPF
660 670 680 690 700
DVYHKARGLR WPVVDGKETL WRYREGSDPY VKPGTGFQFY GNPDGKAVIF
710 720 730 740 750
ALPYEPPPEA PDKEYPFWLS TGRVLEHWHS GSMTRRVPEL YKAFPEAVCF
760 770 780 790 800
MHPDDAQALG VRRGVEVEVV SRRGKMRTRV ETRGRDKPPR GLVFVPWFDA
810 820 830
GQLINKVTLD ATDPISFQTD FKKCAVKIVK V
Length:831
Mass (Da):93,168
Last modified:October 1, 2003 - v1
Checksum:i7A9ED7B93B241585
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640431 Genomic DNA. Translation: CAE37995.1.
RefSeqiWP_010928685.1. NC_002928.3.

Genome annotation databases

EnsemblBacteriaiCAE37995; CAE37995; BPP2702.
KEGGibpa:BPP2702.

Similar proteinsi

Entry informationi

Entry nameiNAPA_BORPA
AccessioniPrimary (citable) accession number: Q7W733
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: October 1, 2003
Last modified: January 31, 2018
This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families