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Protein

Respiratory nitrate reductase beta chain

Gene

narH

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 beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit.By similarity1 Publication

Catalytic activityi

Nitrite + acceptor = nitrate + reduced acceptor.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterBy similarityNote: Binds 3 [4Fe-4S] clusters per subunit.By similarity
  • [3Fe-4S] clusterBy similarityNote: Binds 1 [3Fe-4S] cluster per subunit.By similarity

Enzyme regulationi

Inhibited by micromolar concentrations of azide.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi12Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi15Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi18Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi22Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi39Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi42Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi47Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi51Iron-sulfur 4 (3Fe-4S)By similarity1
Metal bindingi73Iron-sulfur 4 (3Fe-4S)By similarity1
Metal bindingi77Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi81Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi84Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi96Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi100Iron-sulfur 1 (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

3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BRENDAi1.7.99.4. 930.

Names & Taxonomyi

Protein namesi
Recommended name:
Respiratory nitrate reductase beta chain (EC:1.7.99.4)
Alternative name(s):
Respiratory membrane-bound nitrate reductase subunit beta
Gene namesi
Name:narH
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_00002837791 – ›266Respiratory nitrate reductase beta chainAdd BLAST›266

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

ProteinModelPortaliP85098.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 324Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST30
Domaini30 – 614Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST32

Sequence similaritiesi

Contains at least 2 4Fe-4S ferredoxin-type domains.Curated

Keywords - Domaini

Repeat

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
[Graphical view]
PROSITEiPS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Fragments.

P85098-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SQVGMVLNLD KCIGCHTCSV TCKEGMEYAW FNNVESKLCE HCLNPACVAT
60 70 80 90 100
CPSGAIYKRE EDGIVLIDQD KLCISGCPYK CIFCYPRIES GQPTVCSETC
110 120 130 140 150
VGRYLGVLLY DADRIEEAAS TEHETDLLYE RQLDVFLDPN DPKVIEQAIK
160 170 180 190 200
QGIPQNVIDA AQRSPVYKLA LPLHPEYRAA DAGELGSNGI LPDVESLRML
210 220 230 240 250
SAGDTGPVIR SQTVEGVTDT RALEEVGLTE AQAQEMYRYL AIANYEDRFV
260
VPSSHRIDAI NITEVR
Length:266
Mass (Da):29,401
Last modified:April 3, 2007 - v1
Checksum:i67C8E2EA3B0B8D6E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-adjacent residuesi11 – 121 Publication2
Non-adjacent residuesi23 – 241 Publication2
Non-adjacent residuesi37 – 381 Publication2
Non-adjacent residuesi58 – 591 Publication2
Non-adjacent residuesi71 – 721 Publication2
Non-adjacent residuesi80 – 811 Publication2
Non-adjacent residuesi87 – 881 Publication2
Non-adjacent residuesi103 – 1041 Publication2
Non-adjacent residuesi114 – 1151 Publication2
Non-adjacent residuesi131 – 1321 Publication2
Non-adjacent residuesi143 – 1441 Publication2
Non-adjacent residuesi150 – 1511 Publication2
Non-adjacent residuesi163 – 1641 Publication2
Non-adjacent residuesi168 – 1691 Publication2
Non-adjacent residuesi178 – 1791 Publication2
Non-adjacent residuesi198 – 1991 Publication2
Non-adjacent residuesi210 – 2111 Publication2
Non-adjacent residuesi221 – 2221 Publication2
Non-adjacent residuesi238 – 2391 Publication2
Non-adjacent residuesi248 – 2491 Publication2
Non-adjacent residuesi256 – 2571 Publication2
Non-terminal residuei2661 Publication1

Cross-referencesi

3D structure databases

ProteinModelPortaliP85098.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.7.99.4. 930.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
[Graphical view]
PROSITEiPS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNARH_BRASZ
AccessioniPrimary (citable) accession number: P85098
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: October 5, 2016
This is version 35 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.