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Protein

Respiratory nitrate reductase alpha chain

Gene

narG

Organism
Bradyrhizobium sp.
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity
  • Mo-bis(molybdopterin guanine dinucleotide)By similarityNote: 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)DescriptionActionsGraphical viewLength
Metal bindingi29Iron-sulfur (4Fe-4S); via pros nitrogenBy similarity1
Metal bindingi33Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi37Iron-sulfur (4Fe-4S)By similarity1

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

Enzyme and pathway databases

BRENDAi1.7.99.4. 930.

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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002837781 – ›902Respiratory nitrate reductase alpha chainAdd BLAST›902

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.
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.
[Graphical view]
PfamiPF00384. Molybdopterin. 2 hits.
PF01568. Molydop_binding. 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)DescriptionActionsGraphical viewLength
Non-adjacent residuesi6 – 71 Publication2
Non-adjacent residuesi26 – 271 Publication2
Non-adjacent residuesi40 – 411 Publication2
Non-adjacent residuesi66 – 671 Publication2
Non-adjacent residuesi79 – 801 Publication2
Non-adjacent residuesi101 – 1021 Publication2
Non-adjacent residuesi120 – 1211 Publication2
Non-adjacent residuesi126 – 1271 Publication2
Non-adjacent residuesi146 – 1471 Publication2
Non-adjacent residuesi157 – 1581 Publication2
Non-adjacent residuesi170 – 1711 Publication2
Non-adjacent residuesi179 – 1801 Publication2
Non-adjacent residuesi196 – 1971 Publication2
Non-adjacent residuesi212 – 2131 Publication2
Non-adjacent residuesi225 – 2261 Publication2
Non-adjacent residuesi235 – 2361 Publication2
Non-adjacent residuesi252 – 2531 Publication2
Non-adjacent residuesi273 – 2741 Publication2
Non-adjacent residuesi281 – 2821 Publication2
Non-adjacent residuesi290 – 2911 Publication2
Non-adjacent residuesi304 – 3051 Publication2
Non-adjacent residuesi330 – 3311 Publication2
Non-adjacent residuesi338 – 3391 Publication2
Non-adjacent residuesi353 – 3541 Publication2
Non-adjacent residuesi359 – 3601 Publication2
Non-adjacent residuesi367 – 3681 Publication2
Non-adjacent residuesi379 – 3801 Publication2
Non-adjacent residuesi406 – 4071 Publication2
Non-adjacent residuesi420 – 4211 Publication2
Non-adjacent residuesi436 – 4371 Publication2
Non-adjacent residuesi452 – 4531 Publication2
Non-adjacent residuesi465 – 4661 Publication2
Non-adjacent residuesi481 – 4821 Publication2
Non-adjacent residuesi493 – 4941 Publication2
Non-adjacent residuesi507 – 5081 Publication2
Non-adjacent residuesi513 – 5141 Publication2
Non-adjacent residuesi522 – 5231 Publication2
Non-adjacent residuesi529 – 5301 Publication2
Non-adjacent residuesi541 – 5421 Publication2
Non-adjacent residuesi553 – 5541 Publication2
Non-adjacent residuesi573 – 5741 Publication2
Non-adjacent residuesi599 – 6001 Publication2
Non-adjacent residuesi610 – 6111 Publication2
Non-adjacent residuesi622 – 6231 Publication2
Non-adjacent residuesi649 – 6501 Publication2
Non-adjacent residuesi658 – 6591 Publication2
Non-adjacent residuesi668 – 6691 Publication2
Non-adjacent residuesi676 – 6771 Publication2
Non-adjacent residuesi686 – 6871 Publication2
Non-adjacent residuesi700 – 7011 Publication2
Non-adjacent residuesi711 – 7121 Publication2
Non-adjacent residuesi724 – 7251 Publication2
Non-adjacent residuesi733 – 7341 Publication2
Non-adjacent residuesi746 – 7471 Publication2
Non-adjacent residuesi757 – 7581 Publication2
Non-adjacent residuesi773 – 7741 Publication2
Non-adjacent residuesi782 – 7831 Publication2
Non-adjacent residuesi794 – 7951 Publication2
Non-adjacent residuesi807 – 8081 Publication2
Non-adjacent residuesi829 – 8301 Publication2
Non-adjacent residuesi843 – 8441 Publication2
Non-adjacent residuesi852 – 8531 Publication2
Non-adjacent residuesi884 – 8851 Publication2
Non-terminal residuei9021 Publication1

Cross-referencesi

3D structure databases

ProteinModelPortaliP85097.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.7.99.4. 930.

Family and domain databases

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

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 5, 2016
This is version 42 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

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.