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P85097

- NARG_BRASZ

UniProt

P85097 - NARG_BRASZ

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Protein

Respiratory nitrate reductase alpha chain

Gene

narG

Organism
Bradyrhizobium sp.
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

The nitrate reductase enzyme complex allows Bradyrhizobium sp. USDA 3045 to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.By similarity1 Publication

Catalytic activityi

Nitrite + acceptor = nitrate + reduced acceptor.1 Publication

Cofactori

Binds 1 4Fe-4S cluster per subunit.By similarity
Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.By similarity

Enzyme regulationi

Inhibited by micromolar concentrations of azide.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi29 – 291Iron-sulfur (4Fe-4S); via pros nitrogenBy similarity
Metal bindingi33 – 331Iron-sulfur (4Fe-4S)By similarity
Metal bindingi37 – 371Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. nitrate assimilation Source: UniProtKB-KW
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:
Respiratory nitrate reductase alpha chain (EC:1.7.99.4)
Alternative name(s):
Respiratory membrane-bound nitrate reductase subunit alpha
Gene namesi
Name:narG
OrganismiBradyrhizobium sp.
Taxonomic identifieri376 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Subcellular locationi

Cell membrane 1 Publication. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›902›902Respiratory nitrate reductase alpha chainPRO_0000283778Add
BLAST

Expressioni

Inductioni

Induced by anaerobiosis, there is no significant expression in an aerobic environment. Expression is further induced in the presence of nitrate or nitrite.1 Publication

Interactioni

Subunit structurei

Heterotrimer composed of an alpha, a beta and a gamma chain. Alpha and beta are catalytic chains; gamma chains are involved in binding the enzyme complex to the cytoplasmic membrane.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP85097.
SMRiP85097. Positions 2-900.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR028189. Nitr_red_alph_N.
[Graphical view]
PfamiPF00384. Molybdopterin. 2 hits.
PF01568. Molydop_binding. 1 hit.
PF14710. Nitr_red_alph_N. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
PROSITEiPS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragments.

P85097-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
FSPIDRYNDN HTQETYEDRE WENVYRSTHG VNCTGSCSWK DGIVTWEGQE
60 70 80 90 100
LNYPTTGPDM PDFEPRGASY SWYLYSANRG VLWSMWQEEL QNNESPLDAW
110 120 130 140 150
KSSWQEVNEL IAASNVYTVK TYGPDRVAGF SPIPAMSMVS YASGARTPDA
160 170 180 190 200
HFFTEVRVVS VSPDFAESTK LCDLWLAPKQ GTDAAMALAM GHVMLREFHL
210 220 230 240 250
DNPSDYFLNY CRQYTDFPFL VTLSKQKGDQ FVADRAADLV DALGQENNPE
260 270 280 290 300
WKPVLWNENT NDFATPHGTM GSRGKWNLEQ RLEDEETGEK LSVLGIEDEI
310 320 330 340 350
GTVRLQLADG STALVTTVYD LTMANYGLER GLGGQEPKDF NDDVPFTPAW
360 370 380 390 400
QEKITGVPRE LIIQIAREFA DNADKTHGRA VLNLVLLVGA QGVNGGGWAH
410 420 430 440 450
YVGQEKLRPA EGWQTIAMAK HMNSTSYFYN HSSQWRYETV TAQELLSPMA
460 470 480 490 500
DKYQHHGDYN VLAARMGWLP SAPQLGTNPL RQAGMSPVDY TVKFAAEQPE
510 520 530 540 550
NGKNHPRNLF VWRSNLLGSS GKGHEYMLKY LLGTENGIQG KQGGVKPEEV
560 570 580 590 600
EWKLSSTCLY SDIVLPTATW YEKDDMNTSD MHPFIHPLSA AVDPAWESKS
610 620 630 640 650
DWDIFTSLSK KFSEVCVGHL GKETDVVTLP IQHDSAAELA QPLDVKDWKG
660 670 680 690 700
ECEPIPGKTM PQIHVVERDY PATYERFTSI GPLMEKGIAW NTQSEMDLLR
710 720 730 740 750
AWAALSEFTG RDHTHLALNK EDEKFRDIQA QPRTVITSPA FTGSEKQSFY
760 770 780 790 800
LDHDMMKDFG ESLLVYRPPI DTRKSRPEVE GKEITLNYLT PHNKGGPIVW
810 820 830 840 850
ISETDARDLG IEDNDWIEVF NSNGALTARV PAGMTMMYHA QERGGIHNSV
860 870 880 890 900
TRPTHMIGGY AQLAYGFNYY GTVGSNRDEF VVVRNINWLD GEGNDQVQES

VK
Length:902
Mass (Da):101,519
Last modified:April 3, 2007 - v1
Checksum:i93540162AA633C66
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-adjacent residuesi6 – 721 Publication
Non-adjacent residuesi26 – 2721 Publication
Non-adjacent residuesi40 – 4121 Publication
Non-adjacent residuesi66 – 6721 Publication
Non-adjacent residuesi79 – 8021 Publication
Non-adjacent residuesi101 – 10221 Publication
Non-adjacent residuesi120 – 12121 Publication
Non-adjacent residuesi126 – 12721 Publication
Non-adjacent residuesi146 – 14721 Publication
Non-adjacent residuesi157 – 15821 Publication
Non-adjacent residuesi170 – 17121 Publication
Non-adjacent residuesi179 – 18021 Publication
Non-adjacent residuesi196 – 19721 Publication
Non-adjacent residuesi212 – 21321 Publication
Non-adjacent residuesi225 – 22621 Publication
Non-adjacent residuesi235 – 23621 Publication
Non-adjacent residuesi252 – 25321 Publication
Non-adjacent residuesi273 – 27421 Publication
Non-adjacent residuesi281 – 28221 Publication
Non-adjacent residuesi290 – 29121 Publication
Non-adjacent residuesi304 – 30521 Publication
Non-adjacent residuesi330 – 33121 Publication
Non-adjacent residuesi338 – 33921 Publication
Non-adjacent residuesi353 – 35421 Publication
Non-adjacent residuesi359 – 36021 Publication
Non-adjacent residuesi367 – 36821 Publication
Non-adjacent residuesi379 – 38021 Publication
Non-adjacent residuesi406 – 40721 Publication
Non-adjacent residuesi420 – 42121 Publication
Non-adjacent residuesi436 – 43721 Publication
Non-adjacent residuesi452 – 45321 Publication
Non-adjacent residuesi465 – 46621 Publication
Non-adjacent residuesi481 – 48221 Publication
Non-adjacent residuesi493 – 49421 Publication
Non-adjacent residuesi507 – 50821 Publication
Non-adjacent residuesi513 – 51421 Publication
Non-adjacent residuesi522 – 52321 Publication
Non-adjacent residuesi529 – 53021 Publication
Non-adjacent residuesi541 – 54221 Publication
Non-adjacent residuesi553 – 55421 Publication
Non-adjacent residuesi573 – 57421 Publication
Non-adjacent residuesi599 – 60021 Publication
Non-adjacent residuesi610 – 61121 Publication
Non-adjacent residuesi622 – 62321 Publication
Non-adjacent residuesi649 – 65021 Publication
Non-adjacent residuesi658 – 65921 Publication
Non-adjacent residuesi668 – 66921 Publication
Non-adjacent residuesi676 – 67721 Publication
Non-adjacent residuesi686 – 68721 Publication
Non-adjacent residuesi700 – 70121 Publication
Non-adjacent residuesi711 – 71221 Publication
Non-adjacent residuesi724 – 72521 Publication
Non-adjacent residuesi733 – 73421 Publication
Non-adjacent residuesi746 – 74721 Publication
Non-adjacent residuesi757 – 75821 Publication
Non-adjacent residuesi773 – 77421 Publication
Non-adjacent residuesi782 – 78321 Publication
Non-adjacent residuesi794 – 79521 Publication
Non-adjacent residuesi807 – 80821 Publication
Non-adjacent residuesi829 – 83021 Publication
Non-adjacent residuesi843 – 84421 Publication
Non-adjacent residuesi852 – 85321 Publication
Non-adjacent residuesi884 – 88521 Publication
Non-terminal residuei902 – 90211 Publication

Cross-referencesi

3D structure databases

ProteinModelPortali P85097.
SMRi P85097. Positions 2-900.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR028189. Nitr_red_alph_N.
[Graphical view ]
Pfami PF00384. Molybdopterin. 2 hits.
PF01568. Molydop_binding. 1 hit.
PF14710. Nitr_red_alph_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50692. SSF50692. 1 hit.
PROSITEi PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Identification of membrane-bound respiratory nitrate reductase from Bradyrhizobium sp. (Lupinus) USDA 3045 by tandem mass spectrometry."
    Polcyn W.
    Submitted (FEB-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION.
    Strain: USDA 30451 Publication.

Entry informationi

Entry nameiNARG_BRASZ
AccessioniPrimary (citable) accession number: P85097
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: October 29, 2014
This is version 34 of the entry and version 1 of the sequence. [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

External Data

Dasty 3