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P24474

- NIRS_PSEAE

UniProt

P24474 - NIRS_PSEAE

Protein

Nitrite reductase

Gene

nirS

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+.
    NH3 + H2O + acceptor = hydroxylamine + reduced acceptor.

    Cofactori

    Binds 2 heme groups per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei72 – 721Heme (covalent)
    Binding sitei75 – 751Heme (covalent)
    Metal bindingi76 – 761Iron (heme axial ligand)
    Metal bindingi113 – 1131Iron (heme axial ligand)
    Metal bindingi207 – 2071Iron (heme D1 proximal ligand)

    GO - Molecular functioni

    1. electron carrier activity Source: InterPro
    2. heme binding Source: InterPro
    3. hydroxylamine reductase activity Source: UniProtKB-EC
    4. metal ion binding Source: UniProtKB-KW
    5. nitrite reductase (NO-forming) activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nitrite reductase (EC:1.7.2.1)
    Alternative name(s):
    Cytochrome cd1
    Cytochrome oxidase
    Hydroxylamine reductase (EC:1.7.99.1)
    Gene namesi
    Name:nirS
    Ordered Locus Names:PA0519
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA0519.

    Subcellular locationi

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 25251 PublicationAdd
    BLAST
    Chaini26 – 568543Nitrite reductasePRO_0000006576Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi208964.PA0519.

    Structurei

    Secondary structure

    1
    568
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi32 – 354
    Helixi44 – 463
    Beta strandi51 – 533
    Helixi58 – 7114
    Helixi73 – 764
    Turni77 – 804
    Beta strandi83 – 864
    Helixi90 – 967
    Helixi98 – 10710
    Beta strandi110 – 1123
    Turni117 – 1204
    Helixi124 – 13310
    Beta strandi134 – 1363
    Helixi146 – 1527
    Beta strandi154 – 1574
    Helixi159 – 1613
    Helixi172 – 1743
    Beta strandi175 – 1806
    Helixi181 – 1833
    Beta strandi185 – 1906
    Turni191 – 1933
    Beta strandi196 – 2016
    Beta strandi206 – 2116
    Beta strandi217 – 2226
    Beta strandi225 – 2317
    Beta strandi234 – 2363
    Beta strandi238 – 2447
    Beta strandi247 – 2548
    Turni261 – 2633
    Beta strandi264 – 27916
    Turni280 – 2823
    Beta strandi285 – 2906
    Beta strandi296 – 2983
    Beta strandi301 – 3033
    Beta strandi307 – 3126
    Beta strandi314 – 32310
    Turni324 – 3274
    Beta strandi328 – 3336
    Beta strandi337 – 3393
    Beta strandi341 – 3466
    Beta strandi354 – 3563
    Beta strandi362 – 3676
    Helixi368 – 3703
    Beta strandi372 – 3776
    Turni378 – 3814
    Beta strandi382 – 3887
    Beta strandi390 – 3934
    Beta strandi399 – 4035
    Turni404 – 4063
    Beta strandi407 – 42418
    Turni427 – 4293
    Turni431 – 4333
    Beta strandi436 – 4427
    Beta strandi444 – 4463
    Beta strandi459 – 4624
    Helixi470 – 4734
    Beta strandi476 – 4805
    Beta strandi489 – 4913
    Helixi493 – 4975
    Beta strandi505 – 5117
    Beta strandi513 – 52311
    Beta strandi526 – 5283
    Beta strandi531 – 5366
    Turni537 – 5404
    Beta strandi541 – 5466
    Beta strandi553 – 5597
    Helixi560 – 5645

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BL9X-ray2.90A/B26-568[»]
    1GJQX-ray2.70A/B26-568[»]
    1HZUX-ray2.70A26-568[»]
    1HZVX-ray2.83A26-568[»]
    1N15X-ray2.90A/B26-568[»]
    1N50X-ray2.90A/B26-568[»]
    1N90X-ray2.90A/B26-568[»]
    1NIRX-ray2.15A/B26-568[»]
    1NNOX-ray2.65A/B26-568[»]
    ProteinModelPortaliP24474.
    SMRiP24474. Positions 30-568.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24474.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 14086Cytochrome cPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 5429N-terminal tailAdd
    BLAST
    Regioni141 – 568428D1-heme domainAdd
    BLAST

    Sequence similaritiesi

    Contains 1 cytochrome c domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2010.
    HOGENOMiHOG000225986.
    KOiK15864.
    OMAiWPPQFVI.
    OrthoDBiEOG6RC3M0.
    PhylomeDBiP24474.

    Family and domain databases

    Gene3Di1.10.760.10. 1 hit.
    2.130.10.10. 1 hit.
    2.140.10.20. 1 hit.
    InterProiIPR009056. Cyt_c-like_dom.
    IPR003143. Cyt_cd1_C.
    IPR011048. Haem_d1.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view]
    PfamiPF13442. Cytochrome_CBB3. 1 hit.
    [Graphical view]
    SUPFAMiSSF46626. SSF46626. 1 hit.
    SSF51004. SSF51004. 1 hit.
    PROSITEiPS51007. CYTC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P24474-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFGKPLVGT LLASLTLLGL ATAHAKDDMK AAEQYQGAAS AVDPAHVVRT    50
    NGAPDMSESE FNEAKQIYFQ RCAGCHGVLR KGATGKPLTP DITQQRGQQY 100
    LEALITYGTP LGMPNWGSSG ELSKEQITLM AKYIQHTPPQ PPEWGMPEMR 150
    ESWKVLVKPE DRPKKQLNDL DLPNLFSVTL RDAGQIALVD GDSKKIVKVI 200
    DTGYAVHISR MSASGRYLLV IGRDARIDMI DLWAKEPTKV AEIKIGIEAR 250
    SVESSKFKGY EDRYTIAGAY WPPQFAIMDG ETLEPKQIVS TRGMTVDTQT 300
    YHPEPRVAAI IASHEHPEFI VNVKETGKVL LVNYKDIDNL TVTSIGAAPF 350
    LHDGGWDSSH RYFMTAANNS NKVAVIDSKD RRLSALVDVG KTPHPGRGAN 400
    FVHPKYGPVW STSHLGDGSI SLIGTDPKNH PQYAWKKVAE LQGQGGGSLF 450
    IKTHPKSSHL YVDTTFNPDA RISQSVAVFD LKNLDAKYQV LPIAEWADLG 500
    EGAKRVVQPE YNKRGDEVWF SVWNGKNDSS ALVVVDDKTL KLKAVVKDPR 550
    LITPTGKFNV YNTQHDVY 568
    Length:568
    Mass (Da):62,653
    Last modified:March 1, 1992 - v1
    Checksum:i20FAE9FFE9127D62
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16452 Genomic DNA. Translation: CAA34471.1.
    AE004091 Genomic DNA. Translation: AAG03908.1.
    X51631 Genomic DNA. Translation: CAA35957.1.
    X51319 Genomic DNA. Translation: CAA35702.1.
    PIRiA32975. OSPSA.
    RefSeqiNP_249210.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG03908; AAG03908; PA0519.
    GeneIDi882217.
    KEGGipae:PA0519.
    PATRICi19835296. VBIPseAer58763_0549.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16452 Genomic DNA. Translation: CAA34471.1 .
    AE004091 Genomic DNA. Translation: AAG03908.1 .
    X51631 Genomic DNA. Translation: CAA35957.1 .
    X51319 Genomic DNA. Translation: CAA35702.1 .
    PIRi A32975. OSPSA.
    RefSeqi NP_249210.1. NC_002516.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BL9 X-ray 2.90 A/B 26-568 [» ]
    1GJQ X-ray 2.70 A/B 26-568 [» ]
    1HZU X-ray 2.70 A 26-568 [» ]
    1HZV X-ray 2.83 A 26-568 [» ]
    1N15 X-ray 2.90 A/B 26-568 [» ]
    1N50 X-ray 2.90 A/B 26-568 [» ]
    1N90 X-ray 2.90 A/B 26-568 [» ]
    1NIR X-ray 2.15 A/B 26-568 [» ]
    1NNO X-ray 2.65 A/B 26-568 [» ]
    ProteinModelPortali P24474.
    SMRi P24474. Positions 30-568.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208964.PA0519.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG03908 ; AAG03908 ; PA0519 .
    GeneIDi 882217.
    KEGGi pae:PA0519.
    PATRICi 19835296. VBIPseAer58763_0549.

    Organism-specific databases

    PseudoCAPi PA0519.

    Phylogenomic databases

    eggNOGi COG2010.
    HOGENOMi HOG000225986.
    KOi K15864.
    OMAi WPPQFVI.
    OrthoDBi EOG6RC3M0.
    PhylomeDBi P24474.

    Miscellaneous databases

    EvolutionaryTracei P24474.

    Family and domain databases

    Gene3Di 1.10.760.10. 1 hit.
    2.130.10.10. 1 hit.
    2.140.10.20. 1 hit.
    InterProi IPR009056. Cyt_c-like_dom.
    IPR003143. Cyt_cd1_C.
    IPR011048. Haem_d1.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view ]
    Pfami PF13442. Cytochrome_CBB3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46626. SSF46626. 1 hit.
    SSF51004. SSF51004. 1 hit.
    PROSITEi PS51007. CYTC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nitrite reductase from Pseudomonas aeruginosa: sequence of the gene and the protein."
      Silvestrini M.C., Galeotti C.L., Gervais M., Schinina E., Barra D., Bossa F., Brunori M.
      FEBS Lett. 254:33-38(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-70.
      Strain: NTCC 6750.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
    3. "Cloning and sequencing of the gene encoding cytochrome c-551 from Pseudomonas aeruginosa."
      Arai H., Sanbongi Y., Igarashi Y., Kodama T.
      FEBS Lett. 261:196-198(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 462-568.
    4. "The structural gene for cytochrome c551 from Pseudomonas aeruginosa. The nucleotide sequence shows a location downstream of the nitrite reductase gene."
      Nordling M., Young S., Karlsson B.G., Lundberg L.G.
      FEBS Lett. 259:230-232(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 462-568.
      Strain: ATCC 10145 / DSM 50071 / JCM 5962 / LMG 1242 / NBRC 12689 / NCIMB 8295 / NRRL B-771.
    5. "N-terminal arm exchange is observed in the 2.15 A crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa."
      Nurizzo D., Silvestrini M.-C., Mathieu M., Cutruzzola F., Bourgeois D., Fueloep V., Hajdu J., Brunori M., Tegoni M., Cambillau C.
      Structure 5:1157-1171(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
      Strain: NTCC 6750.
    6. "Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa."
      Nurizzo D., Cutruzzola F., Arese M., Bourgeois D., Brunori M., Cambillau C., Tegoni M.
      Biochemistry 37:13987-13996(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
      Strain: NTCC 6750.
    7. "Does the reduction of c heme trigger the conformational change of crystalline nitrite reductase?"
      Nurizzo D., Cutruzzola F., Arese M., Bourgeois D., Brunori M., Cambillau C., Tegoni M.
      J. Biol. Chem. 274:14997-15004(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
      Strain: NTCC 6750.
    8. "The nitrite reductase from Pseudomonas aeruginosa: essential role of two active-site histidines in the catalytic and structural properties."
      Cutruzzola F., Brown K., Wilson E.K., Bellelli A., Arese M., Tegoni M., Cambillau C., Brunori B.
      Proc. Natl. Acad. Sci. U.S.A. 98:2232-2237(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF H394A AND H352A MUTANTS.
    9. "Domain swing upon His to Ala mutation in nitrite reductase of Pseudomonas aeruginosa."
      Brown K., Roig-Zamboni V., Cutruzzola F., Arese M., Sun W., Brunori M., Cambillau C., Tegoni M.
      J. Mol. Biol. 312:541-554(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF H394A AND H352A MUTANTS.

    Entry informationi

    Entry nameiNIRS_PSEAE
    AccessioniPrimary (citable) accession number: P24474
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 126 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3