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 27-MAR-2024, entry version 171. 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; Pseudomonadota; 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 / RC 1C / 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 / RC NCIMB 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 208964.PA0519; -. DR DrugBank; DB03317; Ferroheme C. DR DrugBank; DB03469; Heme D. DR PaxDb; 208964-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 OrthoDB; 5290932at2; -. DR PhylomeDB; P24474; -. DR BioCyc; PAER208964:G1FZ6-524-MONOMER; -. 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; 2.140.10.20; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1. DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 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; PF02239; Cytochrom_D1; 1. DR Pfam; PF13442; Cytochrome_CBB3; 1. DR SUPFAM; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1. DR SUPFAM; SSF46626; Cytochrome c; 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 //