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P85098

- NARH_BRASZ

UniProt

P85098 - NARH_BRASZ

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Protein

Respiratory nitrate reductase beta chain

Gene

narH

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 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

Binds 3 4Fe-4S clusters per subunit.By similarity
Binds 1 3Fe-4S cluster per subunit.By similarity

Enzyme regulationi

Inhibited by micromolar concentrations of azide.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi12 – 121Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi15 – 151Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi18 – 181Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi22 – 221Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi39 – 391Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi42 – 421Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi47 – 471Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi51 – 511Iron-sulfur 4 (3Fe-4S)By similarity
Metal bindingi73 – 731Iron-sulfur 4 (3Fe-4S)By similarity
Metal bindingi77 – 771Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi81 – 811Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi84 – 841Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi96 – 961Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi100 – 1001Iron-sulfur 1 (4Fe-4S)By similarity

GO - Molecular functioni

  1. 3 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  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

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

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

  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 – ›266›266Respiratory nitrate reductase beta chainPRO_0000283779Add
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

ProteinModelPortaliP85098.
SMRiP85098. Positions 1-256.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 32304Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini30 – 61324Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Non-adjacent residuesi11 – 1221 Publication
Non-adjacent residuesi23 – 2421 Publication
Non-adjacent residuesi37 – 3821 Publication
Non-adjacent residuesi58 – 5921 Publication
Non-adjacent residuesi71 – 7221 Publication
Non-adjacent residuesi80 – 8121 Publication
Non-adjacent residuesi87 – 8821 Publication
Non-adjacent residuesi103 – 10421 Publication
Non-adjacent residuesi114 – 11521 Publication
Non-adjacent residuesi131 – 13221 Publication
Non-adjacent residuesi143 – 14421 Publication
Non-adjacent residuesi150 – 15121 Publication
Non-adjacent residuesi163 – 16421 Publication
Non-adjacent residuesi168 – 16921 Publication
Non-adjacent residuesi178 – 17921 Publication
Non-adjacent residuesi198 – 19921 Publication
Non-adjacent residuesi210 – 21121 Publication
Non-adjacent residuesi221 – 22221 Publication
Non-adjacent residuesi238 – 23921 Publication
Non-adjacent residuesi248 – 24921 Publication
Non-adjacent residuesi256 – 25721 Publication
Non-terminal residuei266 – 26611 Publication

Cross-referencesi

3D structure databases

ProteinModelPortali P85098.
SMRi P85098. Positions 1-256.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR017896. 4Fe4S_Fe-S-bd.
[Graphical view ]
Pfami PF13247. Fer4_11. 1 hit.
[Graphical view ]
PROSITEi PS51379. 4FE4S_FER_2. 2 hits.
[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 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 29, 2014
This is version 28 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