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
Nitratiruptor sp. (strain SB155-2)
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 bindingi47Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi50Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi54Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi82Iron-sulfur (4Fe-4S)UniRule annotation1
Binding sitei84Mo-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 sitei424Mo-bis(molybdopterin guanine dinucleotide); via amide nitrogenUniRule annotation1
Binding sitei428Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei534Mo-bis(molybdopterin guanine dinucleotide); via amide nitrogenUniRule annotation1
Binding sitei582Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei609Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei902Substrate; via amide nitrogenUniRule annotation1
Binding sitei910Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei927Mo-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

BioCyciNSP387092:G1G2O-1927-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic nitrate reductaseUniRule annotation (EC:1.9.6.1UniRule annotation)
Gene namesi
Name:napAUniRule annotation
Ordered Locus Names:NIS_1808
OrganismiNitratiruptor sp. (strain SB155-2)
Taxonomic identifieri387092 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaNitratiruptor
Proteomesi

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_100006972132 – 936Periplasmic nitrate reductaseUniRule annotationAdd BLAST905

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

Protein-protein interaction databases

STRINGi387092.NIS_1808

Structurei

3D structure databases

ProteinModelPortaliA6Q604
SMRiA6Q604
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 964Fe-4S Mo/W bis-MGD-typeUniRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni214 – 221Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotation8
Regioni246 – 250Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotation5
Regioni559 – 560Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotation2
Regioni826 – 835Mo-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

eggNOGiENOG4107QIW Bacteria
COG0243 LUCA
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
IPR019546 TAT_signal_bac_arc
PANTHERiPTHR11615:SF123 PTHR11615:SF123, 2 hits
PfamiView protein in Pfam
PF04879 Molybdop_Fe4S4, 1 hit
PF00384 Molybdopterin, 1 hit
PF01568 Molydop_binding, 1 hit
PF10518 TAT_signal, 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.

A6Q604-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSRRDFLK SSAAAAAASA VGLSVPKEVE AASKEAQKGW RWDKAVCRFC
60 70 80 90 100
GTGCGIMIAT KDDRIVAVKG DPLAPVNRGL NCIKGYFTAK IMYGADRLKT
110 120 130 140 150
PLLRMNDKGE FDKKGKFRPV SWKRAFDEME KQFRKAYNEL GPTGVAFFGS
160 170 180 190 200
GQYTVMEGYA AAKLMKAGFR SNNIDPNARH CMASAVAGFI QTFGIDEPAG
210 220 230 240 250
CYDDIELTDT IVLWGSNMAE MHPILWARCT DRKLSDPNKV KVVVLSTYTH
260 270 280 290 300
RSCDLADDVI IFKPNTDLAI WNYIARSIVY DHPDAIDWNF VKEYCVFATG
310 320 330 340 350
YPDIGYGMRN PKRAEELGYS KKEMQTVWHQ DHKKLSEDEK RALAPFGYGN
360 370 380 390 400
ADVMKMKHVK AAGKHWAISF EEFKKSLEPY TLDYVAKVAK GDPDESLESF
410 420 430 440 450
KAKLQRLKDL YVEKGRKVVS FWTMGMNQHT RGTWDNELSY VVHFLLGKQA
460 470 480 490 500
LPGSGAFSLT GQPSACGTAR EVGTFAHRLP ADMVVFNPKH RAIAEKIWKL
510 520 530 540 550
PKGTINPKVG SHIVKIMRDL EDGKIKFAWV HVCNPWQDTA NANHWIKAAR
560 570 580 590 600
DMDNFIVVSD GYPGISAKVA DLILPSAMIY EKWGAYGNAE RRTQHWRQQV
610 620 630 640 650
TPVGDAMPDI WQYTEFAKRF KLKDVWKEWK LPDGTVLPNV LDEAKKMGYS
660 670 680 690 700
EDDTLFDVLF ANDYYRSFKW PDPIGEGFLN TEAEGDKRNV IGADGKPWKG
710 720 730 740 750
YGFFIQKALW EEYRKFGEGR GHDYAPFDVY HKVRGLRWPV VNGKDTPWRF
760 770 780 790 800
NVNYDPYAKR EKELGHVKGE FAFYGHALKV IPQGSLTGPD KNKPKIHLPN
810 820 830 840 850
KAKIFARPYM EPPEVPDNEY DTWLCTGRVL EHWHSGTMTM RVPELYRAVP
860 870 880 890 900
EALCYMHPED AKKRGVKRGD LVVIESRRGK CKARVETRGR NRPPRGLVFV
910 920 930
PWFDERVYIN LVTLDATCPI SKQTDYKKCA VKIYKA
Length:936
Mass (Da):106,390
Last modified:August 21, 2007 - v1
Checksum:i7171B3121E2C1E10
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009178 Genomic DNA Translation: BAF70913.1
RefSeqiWP_012083176.1, NC_009662.1

Genome annotation databases

EnsemblBacteriaiBAF70913; BAF70913; NIS_1808
KEGGinis:NIS_1808

Similar proteinsi

Entry informationi

Entry nameiNAPA_NITSB
AccessioniPrimary (citable) accession number: A6Q604
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: March 28, 2018
This is version 69 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health