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Protein

Periplasmic nitrate reductase

Gene

napA

Organism
Paracoccus pantotrophus (Thiosphaera pantotropha)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

Enzyme and pathway databases

BRENDAi1.9.6.1 4531

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic nitrate reductaseUniRule annotation (EC:1.9.6.1UniRule annotation)
Gene namesi
Name:napAUniRule annotation
OrganismiParacoccus pantotrophus (Thiosphaera pantotropha)
Taxonomic identifieri82367 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Subcellular locationi

  • Periplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Tat-type signalUniRule annotationAdd BLAST31
ChainiPRO_000001917232 – 831Periplasmic 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

PRIDEiQ56350

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ56350
SMRiQ56350
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

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.

Q56350-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTISRRDLLK AQAAGIAAMA ANIPLSSQAP AVPGGVESLQ ITWSKAPCRF
60 70 80 90 100
CGTGCGVMVG VKEGRVVATH GDLLAEVNRG LNCVKGYFLS KIMYGADRLT
110 120 130 140 150
QPLLRKKDGV YAKDGEFTPV SWEEAFDTMA AQAKRVLRDK GPTALGMFGS
160 170 180 190 200
GQWTIFEGYA ATKLMRAGFR SNNLDPNARH CMASAAYAFM RTFGMDEPMG
210 220 230 240 250
CYDDFEAADA FVLWGSNMAE MHPILWTRVA DRRLGHPHVK VAVLSTFTHR
260 270 280 290 300
SSDLADIPIV FKPGTDLAIL NYIANHIIQT GRVNRDFVDR HTTFVAGATG
310 320 330 340 350
IGYGLRDDDP REMAARTAED PAATTPSTFE EFAELVSEYT LDKVSELSGV
360 370 380 390 400
EPAFLEQLAE LYADPDRKVM SLWTMGFNQH VRGVWANQMV YNLHLLTGKI
410 420 430 440 450
SEPGNSPFSL TGQASACGTA RQVGTFRHRL PSDMTVTNPE RRQDAEEIWR
460 470 480 490 500
IPHGVIPEQP GLHAVAQDRA LHDGTLNFYW IQVNNNLQAS PNNDGEAWPG
510 520 530 540 550
YRNPDNFIVV SDAYPTVTAL AADLILPAAM WVEKEGAYGN AERRTHVWHQ
560 570 580 590 600
LVEAPGEARS DLWQMMEFST RFTTDEVWPE EILAANPNYR GQSLFDVLFR
610 620 630 640 650
NGSVDRFDLS ELNPVTPTAE SNAFGFYVQK GLFEEYAPFG RGHGHDLAPY
660 670 680 690 700
DTYHEVRGLR WPVVDGKETL WRYREGLDPY VEPGAGVQFY GNPDGKARII
710 720 730 740 750
AVPYEPPAEP PDEEYNIWLV TGRVLEHWHS GSMTMRVPEL YRAFPGARCF
760 770 780 790 800
MNPEDARDMG FNQGAEVRIV SRRGEIRSRV ETRGRNRMPR GVVFVPWFDA
810 820 830
SQLINKVTLD ATDPISKQTD FKKCAVKILP V
Length:831
Mass (Da):92,618
Last modified:November 1, 1996 - v1
Checksum:iED78963BD2DA2144
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti128T → D AA sequence (PubMed:7639719).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36773 Genomic DNA Translation: CAA85346.1
PIRiS50163

Similar proteinsi

Entry informationi

Entry nameiNAPA_PARPN
AccessioniPrimary (citable) accession number: Q56350
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 105 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

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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