NIRS_PSEST
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 03-AUG-2022, entry version 120.
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 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC 568 / 218 / ZoBell 632;
RX 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 respiration
RT of Pseudomonas stutzeri consists of a cluster of mono-, di-, and tetraheme
RT proteins.";
RL FEBS Lett. 279:205-209(1991).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-
CC [cytochrome c] + 2 H(+) + nitrite; Xref=Rhea:RHEA:15233, Rhea:RHEA-
CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine;
CC Xref=Rhea:RHEA:22052, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15429, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:28938; EC=1.7.99.1;
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:P24474};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000250|UniProtKB:P24474};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P24474};
CC Note=Binds 1 heme d1 group per subunit. {ECO:0000250|UniProtKB:P24474};
CC -!- SUBUNIT: Homodimer in solution.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: By anaerobic conditions. Induced by nitrite, repressed by
CC nitrate, and inhibited by oxygen.
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DR EMBL; X53676; CAA40150.1; -; Genomic_DNA.
DR PIR; S13613; OSPSZ.
DR RefSeq; WP_003279945.1; NZ_CP036186.1.
DR AlphaFoldDB; P24040; -.
DR SMR; P24040; -.
DR STRING; 32042.PstZobell_00967; -.
DR KEGG; ag:CAA40150; -.
DR eggNOG; COG2010; Bacteria.
DR BioCyc; MetaCyc:MON-201; -.
DR BRENDA; 1.7.2.1; 5158.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0050418; F:hydroxylamine reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.760.10; -; 1.
DR Gene3D; 2.140.10.20; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR003143; Cyt_cd1_C_sf.
DR InterPro; IPR011048; Haem_d1_sf.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF51004; SSF51004; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Oxidoreductase; Periplasm; Signal; Transport.
FT SIGNAL 1..26
FT CHAIN 27..560
FT /note="Nitrite reductase"
FT /id="PRO_0000006577"
FT DOMAIN 30..126
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 27..29
FT /note="N-terminal tail"
FT REGION 61..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..560
FT /note="D1-heme domain"
FT BINDING 47
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P24474"
FT BINDING 50
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P24474"
FT BINDING 51
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P24474"
FT BINDING 97
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /evidence="ECO:0000250|UniProtKB:P24474"
FT BINDING 101
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P24474"
FT BINDING 193
FT /ligand="heme d1"
FT /ligand_id="ChEBI:CHEBI:60549"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000250|UniProtKB:P24474"
FT BINDING 236
FT /ligand="heme d1"
FT /ligand_id="ChEBI:CHEBI:60549"
FT /evidence="ECO:0000250|UniProtKB:P24474"
FT BINDING 237
FT /ligand="heme d1"
FT /ligand_id="ChEBI:CHEBI:60549"
FT /evidence="ECO:0000250|UniProtKB:P24474"
FT BINDING 256
FT /ligand="heme d1"
FT /ligand_id="ChEBI:CHEBI:60549"
FT /evidence="ECO:0000250|UniProtKB:P24474"
FT BINDING 382
FT /ligand="heme d1"
FT /ligand_id="ChEBI:CHEBI:60549"
FT /evidence="ECO:0000250|UniProtKB:P24474"
FT BINDING 500
FT /ligand="heme d1"
FT /ligand_id="ChEBI:CHEBI:60549"
FT /evidence="ECO:0000250|UniProtKB:P24474"
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
