Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Periplasmic nitrate reductase

Gene

napA

Organism
Vibrio fischeri (strain MJ11)
Status
Reviewed-Annotation score: -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 sitei374Mo-bis(molybdopterin guanine dinucleotide); via amide nitrogenUniRule annotation1
Binding sitei378Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei484Mo-bis(molybdopterin guanine dinucleotide); via amide nitrogenUniRule annotation1
Binding sitei533Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei560Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei794Substrate; via amide nitrogenUniRule annotation1
Binding sitei802Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei819Mo-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:VFMJ11_2039
OrganismiVibrio fischeri (strain MJ11)
Taxonomic identifieri388396 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio
Proteomesi
  • UP000001857 Componenti: Chromosome I

Subcellular locationi

  • Periplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Tat-type signalUniRule annotationAdd BLAST29
ChainiPRO_100018637830 – 829Periplasmic nitrate reductaseUniRule annotationAdd BLAST800

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

Proteomic databases

PRIDEiB5FGW1

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliB5FGW1
SMRiB5FGW1
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
Regioni510 – 511Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotation2
Regioni718 – 727Mo-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
OMAiTQHWRQQ
OrthoDBiPOG091H060P

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
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
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.

B5FGW1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMTRRAFVK ANAAASAAAV AGVTLPASAT NLIVSSDQTK IKWDKAPCRF
60 70 80 90 100
CGTGCSVLVG TQNGRVVATQ GDPEAPVNKG LNCIKGYFLS KIMYGKDRVQ
110 120 130 140 150
TPMLRMKDGQ YNKDGDFAPV SWDVALDTMA EKWKAALKKH GPTGVGMFGS
160 170 180 190 200
GQWTVMEGYA AVKLMKAGFR SNNIDPNARH CMASAVGAFM RTFGIDEPMG
210 220 230 240 250
CYDDFENADS FVLWGSNMAE MHPVLWTRIS DRRLSHPHVK VNVLSTYYHR
260 270 280 290 300
SFELADKGYI FEPQSDLAIA NFIANYIIQN NAVNWDFVNK HTNFKQATTD
310 320 330 340 350
IGYGLRDDDP IQMEAANPNS GAMSSISFEE YKKSVAPYTA QKASEMSGVS
360 370 380 390 400
EEDLITLAKQ YADPKTKVMS LWTMGMNQHT RGVWMNSLVY NIHLLTGKIA
410 420 430 440 450
TPGNSPFSLT GQPSACGTAR EVGTFSHRLP ADMVVANPKH RAISEKIWKL
460 470 480 490 500
PEGTLNGKPG AHAVVQDRML KDGKINAYWV MCNNNMQAGP NINTERLPGY
510 520 530 540 550
RNPENFIVCS DPYPTATAQA ADLILPTAMW VEKEGAYGNA ERRTQAWYQQ
560 570 580 590 600
VQAKGEAKSD LWQIMEFSKR FKVEEVWGEE LVAKAPEYRG KTMYDILFKN
610 620 630 640 650
GQVDAFPLSE AQELNDDAKA QGFYVQKGLF EEYASFGRGH GHDLAPYDTY
660 670 680 690 700
HTVRGLRWPV VDGKETLWRF KEGSDPYAKK GSDWDFYGKP DGKALIISAP
710 720 730 740 750
YEAPPEVPND EFDMWLCTGR VLEHWHTGTM TRRVPELYKA VPDALCYIHP
760 770 780 790 800
ADAKKRNLRR GDEVLISNKR GEVRVRVETR GRNRPPEGLV FVPFFDARIL
810 820
INKLILDATD PLSKQTDFKK CPVKITKIA
Length:829
Mass (Da):92,594
Last modified:October 14, 2008 - v1
Checksum:i5F9C417D6C0B0950
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001139 Genomic DNA Translation: ACH65259.1
RefSeqiWP_012532927.1, NC_011184.1

Genome annotation databases

EnsemblBacteriaiACH65259; ACH65259; VFMJ11_2039
KEGGivfm:VFMJ11_2039

Similar proteinsi

Entry informationi

Entry nameiNAPA_VIBFM
AccessioniPrimary (citable) accession number: B5FGW1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 14, 2008
Last modified: May 23, 2018
This is version 67 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health