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P39185

- NAPA_CUPNH

UniProt

P39185 - NAPA_CUPNH

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Protein

Periplasmic nitrate reductase

Gene

napA

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein NapC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism.

Catalytic activityi

Nitrite + acceptor = nitrate + reduced acceptor.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)Note: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi48 – 481Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi51 – 511Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi55 – 551Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi83 – 831Iron-sulfur (4Fe-4S)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. electron carrier activity Source: UniProtKB-HAMAP
  3. iron ion binding Source: UniProtKB-HAMAP
  4. molybdenum ion binding Source: InterPro
  5. nitrate reductase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-HAMAP
  2. nitrate assimilation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Nitrate assimilation, Transport

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyciCNEC381666:GJUJ-6487-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic nitrate reductaseUniRule annotation (EC:1.7.99.4UniRule annotation)
Gene namesi
Name:napAUniRule annotation
Ordered Locus Names:PHG211
Encoded oniPlasmid megaplasmid pHG10 Publication
OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Taxonomic identifieri381666 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000008210: Plasmid megaplasmid pHG1

Subcellular locationi

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Tat-type signal1 PublicationUniRule annotationAdd
BLAST
Chaini30 – 831802Periplasmic nitrate reductasePRO_0000019168Add
BLAST

Post-translational modificationi

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Expressioni

Inductioni

Expressed independently of nitrate induction and anaerobiosis.

Interactioni

Subunit structurei

Interacts with NapB.UniRule annotation

Protein-protein interaction databases

STRINGi381666.PHG211.

Structurei

Secondary structure

1
831
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 478Combined sources
Beta strandi56 – 627Combined sources
Beta strandi65 – 717Combined sources
Turni76 – 805Combined sources
Helixi84 – 874Combined sources
Helixi88 – 914Combined sources
Beta strandi103 – 1075Combined sources
Beta strandi115 – 1195Combined sources
Helixi122 – 13918Combined sources
Helixi142 – 1443Combined sources
Beta strandi145 – 1495Combined sources
Helixi155 – 16612Combined sources
Turni167 – 1693Combined sources
Beta strandi174 – 1763Combined sources
Helixi177 – 1804Combined sources
Helixi183 – 19311Combined sources
Helixi202 – 2065Combined sources
Beta strandi209 – 2157Combined sources
Helixi218 – 2214Combined sources
Helixi223 – 23513Combined sources
Beta strandi240 – 2489Combined sources
Helixi250 – 2534Combined sources
Beta strandi256 – 2605Combined sources
Turni263 – 2653Combined sources
Helixi266 – 27914Combined sources
Helixi285 – 2917Combined sources
Beta strandi292 – 2976Combined sources
Helixi310 – 3145Combined sources
Beta strandi324 – 3274Combined sources
Helixi329 – 3379Combined sources
Helixi341 – 3488Combined sources
Helixi352 – 36312Combined sources
Beta strandi369 – 3746Combined sources
Helixi375 – 3784Combined sources
Helixi383 – 39715Combined sources
Beta strandi405 – 4095Combined sources
Turni414 – 4196Combined sources
Helixi420 – 4234Combined sources
Helixi439 – 44810Combined sources
Helixi464 – 4729Combined sources
Beta strandi478 – 4836Combined sources
Helixi486 – 4894Combined sources
Turni493 – 4964Combined sources
Helixi497 – 5026Combined sources
Beta strandi507 – 5148Combined sources
Helixi517 – 5204Combined sources
Beta strandi523 – 5297Combined sources
Helixi531 – 5333Combined sources
Beta strandi536 – 5394Combined sources
Beta strandi543 – 5486Combined sources
Helixi561 – 5699Combined sources
Helixi574 – 5774Combined sources
Helixi580 – 5834Combined sources
Helixi587 – 5893Combined sources
Helixi594 – 5985Combined sources
Beta strandi600 – 6034Combined sources
Helixi609 – 6113Combined sources
Helixi619 – 6246Combined sources
Helixi628 – 64013Combined sources
Turni641 – 6444Combined sources
Helixi650 – 6556Combined sources
Beta strandi659 – 6624Combined sources
Beta strandi670 – 6745Combined sources
Turni675 – 6773Combined sources
Beta strandi697 – 7015Combined sources
Beta strandi713 – 7153Combined sources
Beta strandi717 – 7226Combined sources
Helixi734 – 7363Combined sources
Helixi738 – 7436Combined sources
Beta strandi748 – 7514Combined sources
Helixi753 – 7586Combined sources
Beta strandi766 – 7705Combined sources
Beta strandi775 – 78511Combined sources
Beta strandi792 – 7976Combined sources
Helixi804 – 8063Combined sources
Turni814 – 8163Combined sources
Beta strandi824 – 8307Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ML1X-ray1.60A30-831[»]
3O5AX-ray1.72A30-831[»]
ProteinModelPortaliP39185.
SMRiP39185. Positions 41-828.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 97574Fe-4S Mo/W bis-MGD-typeUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.UniRule annotation
Contains 1 4Fe-4S Mo/W bis-MGD-type domain.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0243.
HOGENOMiHOG000031441.
KOiK02567.
OMAiHAMANVI.
OrthoDBiEOG6CVV7G.

Family and domain databases

HAMAPiMF_01630. Nitrate_reduct.
InterProiIPR009010. Asp_de-COase-like_dom.
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.
[Graphical view]
PfamiPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTiSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
TIGRFAMsiTIGR01706. NAPA. 1 hit.
TIGR01409. TAT_signal_seq. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P39185-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKISRRDFIK QTAITATASV AGVTLPAGAA NFVTDSEVTK LKWSKAPCRF
60 70 80 90 100
CGTGCGVTVA VKDNKVVATQ GDPQAEVNKG LNCVKGYFLS KIMYGQDRLT
110 120 130 140 150
RPLMRMKNGK YDKNGDFAPV TWDQAFDEME RQFKRVLKEK GPTAVGMFGS
160 170 180 190 200
GQWTVWEGYA AAKLYKAGFR SNNIDPNARH CMASAAAGFM RTFGMDEPMG
210 220 230 240 250
CYDDFEAADA FVLWGSNMAE MHPILWTRVT DRRLSHPKTR VVVLSTFTHR
260 270 280 290 300
CFDLADIGII FKPQTDLAML NYIANYIIRN NKVNKDFVNK HTVFKEGVTD
310 320 330 340 350
IGYGLRPDHP LQKAAKNASD PGAAKVITFD EFAKFVSKYD ADYVSKLSAV
360 370 380 390 400
PKAKLDQLAE LYADPNIKVM SLWTMGFNQH TRGTWANNMV YNLHLLTGKI
410 420 430 440 450
ATPGNSPFSL TGQPSACGTA REVGTFSHRL PADMVVTNPK HREEAERIWK
460 470 480 490 500
LPPGTIPDKP GYDAVLQNRM LKDGKLNAYW VQVNNNMQAA ANLMEEGLPG
510 520 530 540 550
YRNPANFIVV SDAYPTVTAL AADLVLPSAM WVEKEGAYGN AERRTQFWHQ
560 570 580 590 600
LVDAPGEARS DLWQLVEFAK RFKVEEVWPP ELIAKKPEYK GKTLYDVLYR
610 620 630 640 650
NGQVDKFPLK DVNAEYHNAE AKAFGFYLQK GLFEEYATFG RGHGHDLAPF
660 670 680 690 700
DAYHEARGLR WPVVNGKETR WRYREGSDPY VKAGTGFQFY GNPDGKAVIF
710 720 730 740 750
ALPYEPPAES PDKEYPYWLV TGRVLEHWHS GSMTRRVPEL YRSFPNAVVF
760 770 780 790 800
MHPEDAKALG LRRGVEVEVV SRRGRMRSRI ETRGRDAPPR GLVFVPWFDA
810 820 830
SQLINKVTLD ATCPISLQTD FKKCAVKIVK V
Length:831
Mass (Da):93,346
Last modified:September 27, 2004 - v2
Checksum:i34CE1CDE6677C42F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1516GMFGSG → ACSAPA in CAA50507. (PubMed:8376334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71385 Genomic DNA. Translation: CAA50507.1.
AY305378 Genomic DNA. Translation: AAP85963.1.
PIRiA48489.
RefSeqiNP_942849.1. NC_005241.1.
WP_011154126.1. NC_005241.1.

Genome annotation databases

EnsemblBacteriaiAAP85963; AAP85963; PHG211.
GeneIDi2656653.
KEGGireh:PHG211.
PATRICi35228976. VBIRalEut6770_0159.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71385 Genomic DNA. Translation: CAA50507.1 .
AY305378 Genomic DNA. Translation: AAP85963.1 .
PIRi A48489.
RefSeqi NP_942849.1. NC_005241.1.
WP_011154126.1. NC_005241.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ML1 X-ray 1.60 A 30-831 [» ]
3O5A X-ray 1.72 A 30-831 [» ]
ProteinModelPortali P39185.
SMRi P39185. Positions 41-828.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 381666.PHG211.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAP85963 ; AAP85963 ; PHG211 .
GeneIDi 2656653.
KEGGi reh:PHG211.
PATRICi 35228976. VBIRalEut6770_0159.

Phylogenomic databases

eggNOGi COG0243.
HOGENOMi HOG000031441.
KOi K02567.
OMAi HAMANVI.
OrthoDBi EOG6CVV7G.

Enzyme and pathway databases

BioCyci CNEC381666:GJUJ-6487-MONOMER.

Family and domain databases

HAMAPi MF_01630. Nitrate_reduct.
InterProi IPR009010. Asp_de-COase-like_dom.
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.
[Graphical view ]
Pfami PF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view ]
SMARTi SM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view ]
SUPFAMi SSF50692. SSF50692. 1 hit.
TIGRFAMsi TIGR01706. NAPA. 1 hit.
TIGR01409. TAT_signal_seq. 1 hit.
PROSITEi PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and function of a periplasmic nitrate reductase in Alcaligenes eutrophus H16."
    Siddiqui R.A., Warnecke-Eberz U., Hengsberger A., Schneider B., Kostka S., Friedrich B.
    J. Bacteriol. 175:5867-5876(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-50.
  2. "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis."
    Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.
    J. Mol. Biol. 332:369-383(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Entry informationi

Entry nameiNAPA_CUPNH
AccessioniPrimary (citable) accession number: P39185
Secondary accession number(s): Q7WXC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: September 27, 2004
Last modified: November 26, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Plasmid, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3