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
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Status
Reviewed-Annotation score: 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)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

GO - Molecular functioni

GO - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic nitrate reductaseUniRule annotation (EC:1.7.99.4UniRule annotation)
Gene namesi
Name:napAUniRule annotation
Ordered Locus Names:RHOS4_40230
ORF Names:RSP_4116
Encoded oniPlasmid pRS241c1 Publication
OrganismiRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Taxonomic identifieri272943 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000002703 Componenti: Plasmid pRS241c

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Tat-type signalUniRule annotationAdd BLAST29
ChainiPRO_000001917130 – 831Periplasmic nitrate reductaseAdd BLAST802

Post-translational modificationi

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Expressioni

Inductioni

Nitrate reductase activity can be induced by nitrate and not repressed by ammonium or oxygen.

Interactioni

Subunit structurei

Interacts with NapB.UniRule annotation1 Publication

Protein-protein interaction databases

IntActiQ53176. 1 interactor.

Structurei

Secondary structure

1831
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi42 – 47Combined sources6
Beta strandi56 – 62Combined sources7
Beta strandi65 – 71Combined sources7
Turni76 – 78Combined sources3
Helixi84 – 87Combined sources4
Helixi88 – 91Combined sources4
Beta strandi103 – 105Combined sources3
Beta strandi107 – 109Combined sources3
Helixi122 – 139Combined sources18
Helixi142 – 144Combined sources3
Beta strandi145 – 149Combined sources5
Helixi155 – 166Combined sources12
Beta strandi174 – 176Combined sources3
Helixi178 – 181Combined sources4
Helixi183 – 193Combined sources11
Helixi204 – 207Combined sources4
Beta strandi209 – 215Combined sources7
Helixi218 – 221Combined sources4
Helixi223 – 235Combined sources13
Beta strandi240 – 248Combined sources9
Helixi250 – 253Combined sources4
Beta strandi256 – 260Combined sources5
Turni263 – 265Combined sources3
Helixi266 – 279Combined sources14
Helixi285 – 291Combined sources7
Beta strandi292 – 296Combined sources5
Helixi310 – 313Combined sources4
Helixi329 – 337Combined sources9
Helixi341 – 348Combined sources8
Helixi352 – 361Combined sources10
Beta strandi369 – 374Combined sources6
Helixi375 – 378Combined sources4
Helixi383 – 397Combined sources15
Beta strandi405 – 409Combined sources5
Turni414 – 419Combined sources6
Helixi420 – 423Combined sources4
Turni431 – 433Combined sources3
Beta strandi434 – 437Combined sources4
Helixi439 – 448Combined sources10
Helixi464 – 472Combined sources9
Beta strandi478 – 483Combined sources6
Helixi486 – 489Combined sources4
Turni491 – 497Combined sources7
Helixi498 – 502Combined sources5
Beta strandi507 – 514Combined sources8
Helixi517 – 520Combined sources4
Beta strandi522 – 528Combined sources7
Helixi531 – 533Combined sources3
Beta strandi536 – 539Combined sources4
Beta strandi543 – 548Combined sources6
Helixi561 – 569Combined sources9
Helixi574 – 577Combined sources4
Helixi580 – 585Combined sources6
Beta strandi587 – 591Combined sources5
Turni594 – 599Combined sources6
Beta strandi601 – 605Combined sources5
Beta strandi607 – 612Combined sources6
Beta strandi614 – 617Combined sources4
Helixi619 – 622Combined sources4
Beta strandi623 – 626Combined sources4
Helixi628 – 637Combined sources10
Beta strandi640 – 644Combined sources5
Helixi652 – 655Combined sources4
Beta strandi659 – 661Combined sources3
Beta strandi670 – 675Combined sources6
Beta strandi692 – 694Combined sources3
Beta strandi697 – 701Combined sources5
Beta strandi713 – 715Combined sources3
Beta strandi717 – 722Combined sources6
Helixi734 – 736Combined sources3
Helixi738 – 743Combined sources6
Beta strandi748 – 750Combined sources3
Helixi753 – 758Combined sources6
Beta strandi766 – 770Combined sources5
Beta strandi775 – 787Combined sources13
Beta strandi792 – 796Combined sources5
Beta strandi800 – 802Combined sources3
Helixi804 – 806Combined sources3
Turni814 – 816Combined sources3
Beta strandi825 – 829Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OGYX-ray3.20A/C/E/G/I/K/M/O30-831[»]
ProteinModelPortaliQ53176.
SMRiQ53176.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53176.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 974Fe-4S Mo/W bis-MGD-typeUniRule annotationAdd BLAST57

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

HOGENOMiHOG000031441.
KOiK02567.
OMAiMARRDFI.
OrthoDBiPOG091H060P.
PhylomeDBiQ53176.

Family and domain databases

HAMAPiMF_01630. Nitrate_reduct. 1 hit.
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.

Q53176-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLTRRDLIK AQAAATAAAA AGLPVSALAQ PVTGGAEALR IRWSKAPCRF
60 70 80 90 100
CGTGCGVMVG TRDGQVVATH GDTQAEVNRG LNCVKGYFLS KIMYGEDRLT
110 120 130 140 150
TPLLRMKDGV YHKEGEFAPV SWDEAFDVMA AQAKRVLKEK GPKAVGMFGS
160 170 180 190 200
GQWTIWEGYA ASKLMRAGFR SNNLDPNARH CMASAATAFM RTFGMDEPMG
210 220 230 240 250
CYDDFEAADA FVLWGSNMAE MHPILWSRLT DRRLSHEHVR VAVLSTFTHR
260 270 280 290 300
SMDLADTPII FRPGTDLAIL NYIAHHIIST GRVNRDFVDR HTNFALGATD
310 320 330 340 350
IGYGLRPEHQ LQLAAKGAAD AGAMTPTDFE TFAALVSEYT LEKAAEISGV
360 370 380 390 400
EPALLEELAE LYADPDRKVM SLWTMGFNQH VRGVWANHMV YNLHLLTGKI
410 420 430 440 450
SEPGNSPFSL TGQPSACGTA REVGTFAHRL PADMVVTNPE HRAHAEEIWK
460 470 480 490 500
LPAGLLPDWV GAHAVEQDRK LHDGEINFYW VQVNNNMQAA PNIDQETYPG
510 520 530 540 550
YRNPENFIVV SDAYPTVTGR CADLVLPAAM WVEKEGAYGN AERRTHFWHQ
560 570 580 590 600
LVEAPGEARS DLWQLMEFSK RFTTDEVWPE EILSAAPAYR GKTLFEVLFA
610 620 630 640 650
NGSVDRFPAS DVNPDHANHE AALFGFYPQK GLFEEYAAFG RGHGHDLAPF
660 670 680 690 700
DTYHEVRGLR WPVVEGEETR WRYREGFDPY VKPGEGLRFY GKPDGRAVIL
710 720 730 740 750
GVPYEPPAES PDEEFGFWLV TGRVLEHWHS GSMTLRVPEL YKAFPGAVCF
760 770 780 790 800
MHPEDARSRG LNRGSEVRVI SRRGEIRTRL ETRGRNRMPR GVVFVPWFDA
810 820 830
SQLINKVTLD ANDPISRQTD FKKCAVKIEA V
Length:831
Mass (Da):92,637
Last modified:January 24, 2006 - v2
Checksum:i74B35640749CC906
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti135R → L in CAA86827 (PubMed:8730872).Curated1
Sequence conflicti141G → A (PubMed:8730872).Curated1
Sequence conflicti143K → E (PubMed:8730872).Curated1
Sequence conflicti252M → S in CAA86827 (PubMed:8730872).Curated1
Sequence conflicti255A → S in CAA86827 (PubMed:8730872).Curated1
Sequence conflicti267L → R in CAA86827 (PubMed:8730872).Curated1
Sequence conflicti369V → W in CAA86827 (PubMed:8730872).Curated1
Sequence conflicti415S → F in CAA86827 (PubMed:8730872).Curated1
Sequence conflicti521C → A in CAA86827 (PubMed:8730872).Curated1
Sequence conflicti660R → H in CAA86827 (PubMed:8730872).Curated1
Sequence conflicti737V → W in CAA86827 (PubMed:8730872).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46806 Genomic DNA. Translation: CAA86827.1.
CP000146 Genomic DNA. Translation: ABA81591.1.
RefSeqiWP_011331398.1. NZ_AKVW01000005.1.
YP_345332.1. NC_007489.1.

Genome annotation databases

EnsemblBacteriaiABA81591; ABA81591; RSP_4116.
GeneIDi3711832.
KEGGirsp:RSP_4116.
PATRICi23149531. VBIRhoSph57909_0178.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46806 Genomic DNA. Translation: CAA86827.1.
CP000146 Genomic DNA. Translation: ABA81591.1.
RefSeqiWP_011331398.1. NZ_AKVW01000005.1.
YP_345332.1. NC_007489.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OGYX-ray3.20A/C/E/G/I/K/M/O30-831[»]
ProteinModelPortaliQ53176.
SMRiQ53176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ53176. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA81591; ABA81591; RSP_4116.
GeneIDi3711832.
KEGGirsp:RSP_4116.
PATRICi23149531. VBIRhoSph57909_0178.

Phylogenomic databases

HOGENOMiHOG000031441.
KOiK02567.
OMAiMARRDFI.
OrthoDBiPOG091H060P.
PhylomeDBiQ53176.

Miscellaneous databases

EvolutionaryTraceiQ53176.

Family and domain databases

HAMAPiMF_01630. Nitrate_reduct. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiNAPA_RHOS4
AccessioniPrimary (citable) accession number: Q53176
Secondary accession number(s): Q3IV43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 24, 2006
Last modified: November 30, 2016
This is version 127 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, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.