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Q83RN5

- NARH_SHIFL

UniProt

Q83RN5 - NARH_SHIFL

Protein

Respiratory nitrate reductase 1 beta chain

Gene

narH

Organism
Shigella flexneri
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    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.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

    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

    Cell membrane By similarity; Peripheral membrane protein By similarity

    GO - Cellular componenti

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

    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.By similarity

    Protein-protein interaction databases

    STRINGi198214.SF1228.

    Structurei

    3D structure databases

    ProteinModelPortaliQ83RN5.
    SMRiQ83RN5. Positions 1-509.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Contains 3 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti402 – 4021I → V in AAP16727. (PubMed:12704152)Curated

    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: October 1, 2014
    This is version 88 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