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Q83RN5

- NARH_SHIFL

UniProt

Q83RN5 - NARH_SHIFL

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Protein

Respiratory nitrate reductase 1 beta chain

Gene
narH, SF1228, S1312
Organism
Shigella flexneri
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

The nitrate reductase enzyme complex allows S.flexneri 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 similarity.

Catalytic activityi

Nitrite + acceptor = nitrate + reduced acceptor.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi16 – 161Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi19 – 191Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi22 – 221Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi26 – 261Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi184 – 1841Iron-sulfur 3 (4Fe-4S) By similarity
Metal bindingi187 – 1871Iron-sulfur 3 (4Fe-4S) By similarity
Metal bindingi192 – 1921Iron-sulfur 3 (4Fe-4S) By similarity
Metal bindingi196 – 1961Iron-sulfur 4 (3Fe-4S) By similarity
Metal bindingi217 – 2171Iron-sulfur 4 (3Fe-4S) By similarity
Metal bindingi223 – 2231Iron-sulfur 4 (3Fe-4S) By similarity
Metal bindingi227 – 2271Iron-sulfur 3 (4Fe-4S) By similarity
Metal bindingi244 – 2441Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi247 – 2471Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi259 – 2591Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi263 – 2631Iron-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 1 beta chain (EC:1.7.99.4)
Gene namesi
Name:narH
Ordered Locus Names:SF1228, S1312
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. nitrate reductase complex Source: InterPro
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 512512Respiratory nitrate reductase 1 beta chainPRO_0000096721Add
BLAST

Proteomic databases

PaxDbiQ83RN5.

Interactioni

Subunit structurei

Dimer of heterotrimers each 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 By similarity.

Protein-protein interaction databases

STRINGi198214.SF1228.

Structurei

3D structure databases

ProteinModelPortaliQ83RN5.
SMRiQ83RN5. Positions 1-509.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 35294Fe-4S ferredoxin-type 1Add
BLAST
Domaini175 – 206324Fe-4S ferredoxin-type 2Add
BLAST
Domaini208 – 237304Fe-4S ferredoxin-type 3Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1140.
HOGENOMiHOG000237353.
KOiK00371.
OMAiPHAWEDQ.
OrthoDBiEOG6X3W4C.

Family and domain databases

Gene3Di1.10.3650.10. 1 hit.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR029263. Nitr_red_bet_C.
IPR006547. NO3_Rdtase_bsu.
[Graphical view]
PfamiPF13247. Fer4_11. 1 hit.
PF14711. Nitr_red_bet_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01660. narH. 1 hit.
PROSITEiPS51379. 4FE4S_FER_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q83RN5-1 [UniParc]FASTAAdd to Basket

« Hide

MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ    50
GFPTDWENQE KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY 100
YEPFDFDYQN LHTAPEGSKS QPIARPRSLI TGERMAKIEK GPNWEDDLGG 150
EFDKLAKDKN FDNIQKAMYS QFENTFMMYL PRLCEHCLNP ACVATCPSGA 200
IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK SEKCIFCYPR 250
IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF 300
LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL 350
PMVWYVPPLS PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK 400
PILRALKRML AMRHYKRAET VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA 450
NYEDRFVVPS SHRELAREAF PEKNGCGFTF GDGCHGSDTK FNLFNSRRID 500
AIDVTSKTEP HP 512
Length:512
Mass (Da):58,080
Last modified:June 1, 2003 - v1
Checksum:iF8AC747E1C0973DB
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti402 – 4021I → V in AAP16727. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN42841.1.
AE014073 Genomic DNA. Translation: AAP16727.1.
RefSeqiNP_707134.1. NC_004337.2.
NP_836920.1. NC_004741.1.

Genome annotation databases

EnsemblBacteriaiAAN42841; AAN42841; SF1228.
AAP16727; AAP16727; S1312.
GeneIDi1024183.
1077691.
KEGGisfl:SF1228.
sfx:S1312.
PATRICi18703866. VBIShiFle31049_1438.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005674 Genomic DNA. Translation: AAN42841.1 .
AE014073 Genomic DNA. Translation: AAP16727.1 .
RefSeqi NP_707134.1. NC_004337.2.
NP_836920.1. NC_004741.1.

3D structure databases

ProteinModelPortali Q83RN5.
SMRi Q83RN5. Positions 1-509.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198214.SF1228.

Proteomic databases

PaxDbi Q83RN5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN42841 ; AAN42841 ; SF1228 .
AAP16727 ; AAP16727 ; S1312 .
GeneIDi 1024183.
1077691.
KEGGi sfl:SF1228.
sfx:S1312.
PATRICi 18703866. VBIShiFle31049_1438.

Phylogenomic databases

eggNOGi COG1140.
HOGENOMi HOG000237353.
KOi K00371.
OMAi PHAWEDQ.
OrthoDBi EOG6X3W4C.

Family and domain databases

Gene3Di 1.10.3650.10. 1 hit.
InterProi IPR017896. 4Fe4S_Fe-S-bd.
IPR029263. Nitr_red_bet_C.
IPR006547. NO3_Rdtase_bsu.
[Graphical view ]
Pfami PF13247. Fer4_11. 1 hit.
PF14711. Nitr_red_bet_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01660. narH. 1 hit.
PROSITEi PS51379. 4FE4S_FER_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiNARH_SHIFL
AccessioniPrimary (citable) accession number: Q83RN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: June 1, 2003
Last modified: June 11, 2014
This is version 87 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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