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Protein

Periplasmic nitrate reductase

Gene

napA

Organism
Histophilus somni (strain 2336) (Haemophilus somnus)
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 bindingi44Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi47Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi51Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi79Iron-sulfur (4Fe-4S)UniRule annotation1
Binding sitei81Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei148Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei173Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei177Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei372Mo-bis(molybdopterin guanine dinucleotide); via amide nitrogenUniRule annotation1
Binding sitei376Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei482Mo-bis(molybdopterin guanine dinucleotide); via amide nitrogenUniRule annotation1
Binding sitei531Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei558Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei793Substrate; via amide nitrogenUniRule annotation1
Binding sitei801Mo-bis(molybdopterin guanine dinucleotide)UniRule annotation1
Binding sitei818Mo-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

BioCyciHSOM228400:G1GB8-507-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:HSM_0493
OrganismiHistophilus somni (strain 2336) (Haemophilus somnus)
Taxonomic identifieri228400 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
Proteomesi
  • UP000008543 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 – 32Tat-type signalUniRule annotationAdd BLAST32
ChainiPRO_500031096133 – 827Periplasmic nitrate reductaseUniRule annotationAdd BLAST795

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

ProteinModelPortaliB0URQ3
SMRiB0URQ3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 934Fe-4S Mo/W bis-MGD-typeUniRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni210 – 217Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotation8
Regioni242 – 246Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotation5
Regioni261 – 263Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotation3
Regioni508 – 509Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotation2
Regioni717 – 726Mo-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
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.

B0URQ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLSRRDFMK ANAALAAASV AGLIIPVKNV NAADTSITWD KAVCRFCGTG
60 70 80 90 100
CAVLVGTKDG RVVASQGDPD AEVNRGLNCI KGYFLPKIMY GKDRLTHPML
110 120 130 140 150
RMKNGQYDKE GEFTPVTWDF AFKTMAEKFK SALKAKGPNG VGMFTSGQST
160 170 180 190 200
IFEGVAKSKL FKAGLLSNNI DPNARHCMAS AAVAFVRTFG IDEPMGCYDD
210 220 230 240 250
IEHADAFVLW GSNMAEMHPI LWSRISDRRL ANPDTVSVNV LSTFEHRSFE
260 270 280 290 300
LADLGILLKP QSDLAILNYI ANYLIENNAI NREFIEKHTK FKRGETDIGY
310 320 330 340 350
GLRPQDPREQ TAKNVKTAGK MYDSSFEEFK KLVAPYTLEK AHEISGVPKE
360 370 380 390 400
QLEKLAKLYA DPNKKVVSYW TMGINQHTRG VWANHLIYNI HLLTGKISLP
410 420 430 440 450
GCGPFSLTGQ PSACGTAREV GTFIHRLPAD LVVIKPEHRK IAEKIWKLPE
460 470 480 490 500
GLISDKLGFH AVAQSRALKD GKMQVLWQMC NNNMQAGPNI NEETYPGWRN
510 520 530 540 550
PDNFIVVSDP YPTVSALSAD LILPTAMWVE KEGAYGNAER RTQFWRQQVK
560 570 580 590 600
APGEAKSDLW QLVEFSKYFT TDEVWPAEIL AKNPAYQGKT LYEVLYLNGQ
610 620 630 640 650
VNQYSNDELK GRLNDEAYHF GFYIQKGLFE EYASFGRGHG HDLADFDTYH
660 670 680 690 700
KARGLRWPVV DGKETLWRYR EGYDPYVKAG EGVSFYGQAD KRAVILAVPY
710 720 730 740 750
EPPAEVPDRK YDLWLTTGRI LEHWHTGSMT RRVPELHRSF PNNLVWMNPN
760 770 780 790 800
DAKKRGLKHG DKIKVISRRG EITSYIDTRG RNKCPEGLIY TTFFDAGQLA
810 820
NKLILDATDP ISKETDFKKC AVKVVKA
Length:827
Mass (Da):93,015
Last modified:April 8, 2008 - v1
Checksum:i161C8DCAACC85DEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000947 Genomic DNA Translation: ACA32139.1
RefSeqiWP_012341329.1, NC_010519.1

Genome annotation databases

EnsemblBacteriaiACA32139; ACA32139; HSM_0493
GeneIDi31486772
KEGGihsm:HSM_0493

Similar proteinsi

Entry informationi

Entry nameiNAPA_HISS2
AccessioniPrimary (citable) accession number: B0URQ3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 8, 2008
Last modified: March 28, 2018
This is version 73 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
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Main funding by: National Institutes of Health