Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P24474

- NIRS_PSEAE

UniProt

P24474 - NIRS_PSEAE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

Functioni

Catalytic activityi

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

Cofactori

hemeNote: 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
Complete GO annotation...

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-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP24474.
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

        10         20         30         40         50
MPFGKPLVGT LLASLTLLGL ATAHAKDDMK AAEQYQGAAS AVDPAHVVRT
60 70 80 90 100
NGAPDMSESE FNEAKQIYFQ RCAGCHGVLR KGATGKPLTP DITQQRGQQY
110 120 130 140 150
LEALITYGTP LGMPNWGSSG ELSKEQITLM AKYIQHTPPQ PPEWGMPEMR
160 170 180 190 200
ESWKVLVKPE DRPKKQLNDL DLPNLFSVTL RDAGQIALVD GDSKKIVKVI
210 220 230 240 250
DTGYAVHISR MSASGRYLLV IGRDARIDMI DLWAKEPTKV AEIKIGIEAR
260 270 280 290 300
SVESSKFKGY EDRYTIAGAY WPPQFAIMDG ETLEPKQIVS TRGMTVDTQT
310 320 330 340 350
YHPEPRVAAI IASHEHPEFI VNVKETGKVL LVNYKDIDNL TVTSIGAAPF
360 370 380 390 400
LHDGGWDSSH RYFMTAANNS NKVAVIDSKD RRLSALVDVG KTPHPGRGAN
410 420 430 440 450
FVHPKYGPVW STSHLGDGSI SLIGTDPKNH PQYAWKKVAE LQGQGGGSLF
460 470 480 490 500
IKTHPKSSHL YVDTTFNPDA RISQSVAVFD LKNLDAKYQV LPIAEWADLG
510 520 530 540 550
EGAKRVVQPE YNKRGDEVWF SVWNGKNDSS ALVVVDDKTL KLKAVVKDPR
560
LITPTGKFNV YNTQHDVY
Length:568
Mass (Da):62,653
Last modified:March 1, 1992 - v1
Checksum:i20FAE9FFE9127D62
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P24474.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 128 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