ID   NIRS_PSEST              Reviewed;         560 AA.
AC   P24040;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-NOV-2008, entry version 65.
DE   RecName: Full=Nitrite reductase;
DE            EC=1.7.2.1;
DE   AltName: Full=Cytochrome cd1;
DE   AltName: Full=Cytochrome oxidase;
DE   AltName: Full=Hydroxylamine reductase;
DE            EC=1.7.99.1;
DE   Flags: Precursor;
GN   Name=nirS;
OS   Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 14405 / 218 / ZoBell;
RX   MEDLINE=91160715; PubMed=2001732; DOI=10.1016/0014-5793(91)80150-2;
RA   Juengst A., Wakabayashi S., Matsubara H., Zumft W.G.;
RT   "The nirSTBM region coding for cytochrome cd1-dependent nitrite
RT   respiration of Pseudomonas stutzeri consists of a cluster of mono-,
RT   di-, and tetraheme proteins.";
RL   FEBS Lett. 279:205-209(1991).
CC   -!- CATALYTIC ACTIVITY: Nitric oxide + H(2)O + ferricytochrome c =
CC       nitrite + ferrocytochrome c + 2 H(+).
CC   -!- CATALYTIC ACTIVITY: NH(3) + H(2)O + acceptor = hydroxylamine +
CC       reduced acceptor.
CC   -!- COFACTOR: Binds 2 heme groups per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer in solution.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- INDUCTION: By anaerobic conditions. Induced by nitrite, repressed
CC       by nitrate, and inhibited by oxygen.
CC   -!- SIMILARITY: Contains 1 cytochrome c domain.
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DR   EMBL; X53676; CAA40150.1; -; Genomic_DNA.
DR   PIR; S13613; OSPSZ.
DR   HSSP; P24474; 1GJQ.
DR   BioCyc; MetaCyc:MON-201; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050418; F:hydroxylamine reductase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0046209; P:nitric oxide metabolic process; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR003143; Cyt_d1_haem.
DR   Gene3D; G3DSA:2.140.10.20; Cyt_d1_haem; 1.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   Pfam; PF02239; Cytochrom_D1; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Heme; Iron;
KW   Metal-binding; Oxidoreductase; Periplasm; Signal; Transport.
FT   SIGNAL        1     26
FT   CHAIN        27    560       Nitrite reductase.
FT                                /FTId=PRO_0000006577.
FT   DOMAIN       30    126       Cytochrome c.
FT   REGION       27     29       N-terminal tail.
FT   REGION      127    560       D1-heme domain.
FT   METAL        51     51       Iron (heme axial ligand) (By similarity).
FT   METAL       101    101       Iron (heme axial ligand) (By similarity).
FT   METAL       193    193       Iron (heme D1 proximal ligand) (By
FT                                similarity).
FT   BINDING      47     47       Heme (covalent) (By similarity).
FT   BINDING      50     50       Heme (covalent) (By similarity).
SQ   SEQUENCE   560 AA;  61993 MW;  476259C35FBFA7A0 CRC64;
     MSNVGKPILA GLIAGLSLLG LAVAQAAAPE MTAEEKEASK QIYFERCAGC HGVLRKGATG
     KNLEPHWSKT EADGKKTEGG TLNLGTKRLE NIIAYGTEGG MVNYDDILTK EEINMMARYI
     QHTPDIPPEF SLQDMKDSWN LIVPVEKRVT KQMNKINLQN VFAVTLRDAG KLALIDGDTH
     KIWKVLESGY AVHISRMSAS GRYVYTTGRD GLTTIIDLWP EEPMTVATVR FGSDMRSVDV
     SKFEGYEDKY LIGGTYWPPQ YSIVDGLTLE PIKVVSTRGQ TVDGEYHPEP RVASIVASHI
     KPEWVVNVKE TGQIILVDYT DLKNLKTTTI ESAKFLHDGG WDYSKRYFMV AANASNKVAA
     VDTKTGKLAA LIDTAKIPHP GRGANFVHPQ FGPVWSTGHL GDDVVSLIST PSEESKYAKY
     KEHNWKVVQE LKMPGAGNLF VKTHPKSKHF WADAPMNPER EVAESVYVFD MNDLSKAPIQ
     LNVAKDSGLP ESKAIRRAVQ PEYNKAGDEV WISLWGGKTD QSAIVIYDDK TLKLKRVITD
     PAVVTPTGKF NVFNTMNDVY
//