NIRS_PSEAE
ID NIRS_PSEAE Reviewed; 568 AA.
AC P24474;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 163.
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; OrderedLocusNames=PA0519;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-70.
RC STRAIN=NTCC 6750;
RX PubMed=2506077; DOI=10.1016/0014-5793(89)81004-x;
RA Silvestrini M.C., Galeotti C.L., Gervais M., Schinina E., Barra D.,
RA Bossa F., Brunori M.;
RT "Nitrite reductase from Pseudomonas aeruginosa: sequence of the gene and
RT the protein.";
RL FEBS Lett. 254:33-38(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 462-568.
RX PubMed=2155133; DOI=10.1016/0014-5793(90)80669-a;
RA Arai H., Sanbongi Y., Igarashi Y., Kodama T.;
RT "Cloning and sequencing of the gene encoding cytochrome c-551 from
RT Pseudomonas aeruginosa.";
RL FEBS Lett. 261:196-198(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 462-568.
RC STRAIN=ATCC 10145 / DSM 50071 / JCM 5962 / LMG 1242 / NBRC 12689 / NCIMB
RC 8295 / NRRL B-771;
RX PubMed=2152881; DOI=10.1016/0014-5793(90)80015-b;
RA Nordling M., Young S., Karlsson B.G., Lundberg L.G.;
RT "The structural gene for cytochrome c551 from Pseudomonas aeruginosa. The
RT nucleotide sequence shows a location downstream of the nitrite reductase
RT gene.";
RL FEBS Lett. 259:230-232(1990).
RN [5] {ECO:0007744|PDB:1NIR}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 26-568 IN COMPLEX WITH HEME C AND
RP HEME D1, AND COFACTOR.
RC STRAIN=NTCC 6750;
RX PubMed=9331415; DOI=10.1016/s0969-2126(97)00267-0;
RA Nurizzo D., Silvestrini M.-C., Mathieu M., Cutruzzola F., Bourgeois D.,
RA Fueloep V., Hajdu J., Brunori M., Tegoni M., Cambillau C.;
RT "N-terminal arm exchange is observed in the 2.15 A crystal structure of
RT oxidized nitrite reductase from Pseudomonas aeruginosa.";
RL Structure 5:1157-1171(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
RC STRAIN=NTCC 6750;
RX PubMed=9760233; DOI=10.1021/bi981348y;
RA Nurizzo D., Cutruzzola F., Arese M., Bourgeois D., Brunori M.,
RA Cambillau C., Tegoni M.;
RT "Conformational changes occurring upon reduction and NO binding in nitrite
RT reductase from Pseudomonas aeruginosa.";
RL Biochemistry 37:13987-13996(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC STRAIN=NTCC 6750;
RX PubMed=10329702; DOI=10.1074/jbc.274.21.14997;
RA Nurizzo D., Cutruzzola F., Arese M., Bourgeois D., Brunori M.,
RA Cambillau C., Tegoni M.;
RT "Does the reduction of c heme trigger the conformational change of
RT crystalline nitrite reductase?";
RL J. Biol. Chem. 274:14997-15004(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF H394A AND H352A MUTANTS.
RX PubMed=11226222; DOI=10.1073/pnas.041365298;
RA Cutruzzola F., Brown K., Wilson E.K., Bellelli A., Arese M., Tegoni M.,
RA Cambillau C., Brunori B.;
RT "The nitrite reductase from Pseudomonas aeruginosa: essential role of two
RT active-site histidines in the catalytic and structural properties.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2232-2237(2001).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF H394A AND H352A MUTANTS.
RX PubMed=11563915; DOI=10.1006/jmbi.2001.4986;
RA Brown K., Roig-Zamboni V., Cutruzzola F., Arese M., Sun W., Brunori M.,
RA Cambillau C., Tegoni M.;
RT "Domain swing upon His to Ala mutation in nitrite reductase of Pseudomonas
RT aeruginosa.";
RL J. Mol. Biol. 312:541-554(2001).
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:0000269|PubMed:9331415};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000269|PubMed:9331415};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:9331415};
CC Note=Binds 1 heme d1 group per subunit. {ECO:0000269|PubMed:9331415};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
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DR EMBL; X16452; CAA34471.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03908.1; -; Genomic_DNA.
DR EMBL; X51631; CAA35957.1; -; Genomic_DNA.
DR EMBL; X51319; CAA35702.1; -; Genomic_DNA.
DR PIR; A32975; OSPSA.
DR RefSeq; NP_249210.1; NC_002516.2.
DR RefSeq; WP_003111532.1; NZ_QZGE01000010.1.
DR PDB; 1BL9; X-ray; 2.90 A; A/B=26-568.
DR PDB; 1GJQ; X-ray; 2.70 A; A/B=26-568.
DR PDB; 1HZU; X-ray; 2.70 A; A=26-568.
DR PDB; 1HZV; X-ray; 2.83 A; A=26-568.
DR PDB; 1N15; X-ray; 2.90 A; A/B=26-568.
DR PDB; 1N50; X-ray; 2.90 A; A/B=26-568.
DR PDB; 1N90; X-ray; 2.90 A; A/B=26-568.
DR PDB; 1NIR; X-ray; 2.15 A; A/B=26-568.
DR PDB; 1NNO; X-ray; 2.65 A; A/B=26-568.
DR PDB; 5GUW; X-ray; 3.20 A; M/N=1-568.
DR PDB; 6TPO; X-ray; 1.86 A; A=26-568.
DR PDB; 6TSI; X-ray; 2.38 A; A/B=26-568.
DR PDBsum; 1BL9; -.
DR PDBsum; 1GJQ; -.
DR PDBsum; 1HZU; -.
DR PDBsum; 1HZV; -.
DR PDBsum; 1N15; -.
DR PDBsum; 1N50; -.
DR PDBsum; 1N90; -.
DR PDBsum; 1NIR; -.
DR PDBsum; 1NNO; -.
DR PDBsum; 5GUW; -.
DR PDBsum; 6TPO; -.
DR PDBsum; 6TSI; -.
DR AlphaFoldDB; P24474; -.
DR SMR; P24474; -.
DR STRING; 287.DR97_3487; -.
DR DrugBank; DB03317; Ferroheme C.
DR DrugBank; DB03469; Heme D.
DR PaxDb; P24474; -.
DR PRIDE; P24474; -.
DR EnsemblBacteria; AAG03908; AAG03908; PA0519.
DR GeneID; 882217; -.
DR KEGG; pae:PA0519; -.
DR PATRIC; fig|208964.12.peg.549; -.
DR PseudoCAP; PA0519; -.
DR HOGENOM; CLU_025262_0_0_6; -.
DR InParanoid; P24474; -.
DR OMA; MPNWGTS; -.
DR PhylomeDB; P24474; -.
DR BioCyc; PAER208964:G1FZ6-524-MON; -.
DR BRENDA; 1.7.2.1; 5087.
DR EvolutionaryTrace; P24474; -.
DR Proteomes; UP000002438; Chromosome.
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; TAS:PseudoCAP.
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 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Oxidoreductase; Periplasm; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:2506077"
FT CHAIN 26..568
FT /note="Nitrite reductase"
FT /id="PRO_0000006576"
FT DOMAIN 55..140
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 26..54
FT /note="N-terminal tail"
FT REGION 141..568
FT /note="D1-heme domain"
FT BINDING 72
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9331415,
FT ECO:0007744|PDB:1NIR"
FT BINDING 75
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:9331415,
FT ECO:0007744|PDB:1NIR"
FT BINDING 76
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:0000269|PubMed:9331415,
FT ECO:0007744|PDB:1NIR"
FT BINDING 96
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /evidence="ECO:0000269|PubMed:9331415,
FT ECO:0007744|PDB:1NIR"
FT BINDING 109
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /evidence="ECO:0000269|PubMed:9331415,
FT ECO:0007744|PDB:1NIR"
FT BINDING 113
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:0000269|PubMed:9331415,
FT ECO:0007744|PDB:1NIR"
FT BINDING 207
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:0000269|PubMed:9331415,
FT ECO:0007744|PDB:1NIR"
FT BINDING 250
FT /ligand="heme d1"
FT /ligand_id="ChEBI:CHEBI:60549"
FT /evidence="ECO:0000269|PubMed:9331415,
FT ECO:0007744|PDB:1NIR"
FT BINDING 251
FT /ligand="heme d1"
FT /ligand_id="ChEBI:CHEBI:60549"
FT /evidence="ECO:0000269|PubMed:9331415,
FT ECO:0007744|PDB:1NIR"
FT BINDING 270
FT /ligand="heme d1"
FT /ligand_id="ChEBI:CHEBI:60549"
FT /evidence="ECO:0000269|PubMed:9331415,
FT ECO:0007744|PDB:1NIR"
FT BINDING 397
FT /ligand="heme d1"
FT /ligand_id="ChEBI:CHEBI:60549"
FT /evidence="ECO:0000269|PubMed:9331415,
FT ECO:0007744|PDB:1NIR"
FT BINDING 508
FT /ligand="heme d1"
FT /ligand_id="ChEBI:CHEBI:60549"
FT /evidence="ECO:0000269|PubMed:9331415,
FT ECO:0007744|PDB:1NIR"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:1NIR"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1NIR"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1HZV"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:6TPO"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:1NIR"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6TPO"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:6TPO"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6TPO"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1HZV"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:6TPO"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6TPO"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:6TPO"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 314..323
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 341..346
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:6TPO"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:1NIR"
FT STRAND 371..377
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 378..381
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:1NIR"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 407..413
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:1HZU"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:6TPO"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 476..480
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:5GUW"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:6TPO"
FT HELIX 493..497
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 504..511
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 515..524
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 530..536
FT /evidence="ECO:0007829|PDB:6TPO"
FT TURN 537..540
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 541..546
FT /evidence="ECO:0007829|PDB:6TPO"
FT STRAND 553..559
FT /evidence="ECO:0007829|PDB:6TPO"
FT HELIX 560..564
FT /evidence="ECO:0007829|PDB:6TPO"
SQ SEQUENCE 568 AA; 62653 MW; 20FAE9FFE9127D62 CRC64;
MPFGKPLVGT LLASLTLLGL ATAHAKDDMK AAEQYQGAAS AVDPAHVVRT NGAPDMSESE
FNEAKQIYFQ RCAGCHGVLR KGATGKPLTP DITQQRGQQY LEALITYGTP LGMPNWGSSG
ELSKEQITLM AKYIQHTPPQ PPEWGMPEMR ESWKVLVKPE DRPKKQLNDL DLPNLFSVTL
RDAGQIALVD GDSKKIVKVI DTGYAVHISR MSASGRYLLV IGRDARIDMI DLWAKEPTKV
AEIKIGIEAR SVESSKFKGY EDRYTIAGAY WPPQFAIMDG ETLEPKQIVS TRGMTVDTQT
YHPEPRVAAI IASHEHPEFI VNVKETGKVL LVNYKDIDNL TVTSIGAAPF LHDGGWDSSH
RYFMTAANNS NKVAVIDSKD RRLSALVDVG KTPHPGRGAN FVHPKYGPVW STSHLGDGSI
SLIGTDPKNH PQYAWKKVAE LQGQGGGSLF IKTHPKSSHL YVDTTFNPDA RISQSVAVFD
LKNLDAKYQV LPIAEWADLG EGAKRVVQPE YNKRGDEVWF SVWNGKNDSS ALVVVDDKTL
KLKAVVKDPR LITPTGKFNV YNTQHDVY
