(data stored in SCRATCH9089 zone)

SWISSPROT: NRFA_PASMU

ID   NRFA_PASMU              Reviewed;         510 AA.
AC   Q9CPL4;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 129.
DE   RecName: Full=Cytochrome c-552 {ECO:0000255|HAMAP-Rule:MF_01182};
DE            EC=1.7.2.2 {ECO:0000255|HAMAP-Rule:MF_01182};
DE   AltName: Full=Ammonia-forming cytochrome c nitrite reductase {ECO:0000255|HAMAP-Rule:MF_01182};
DE            Short=Cytochrome c nitrite reductase {ECO:0000255|HAMAP-Rule:MF_01182};
DE   Flags: Precursor;
GN   Name=nrfA {ECO:0000255|HAMAP-Rule:MF_01182}; OrderedLocusNames=PM0023;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming six
CC       electrons in the process. {ECO:0000255|HAMAP-Rule:MF_01182}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6 [Fe(III)cytochrome c] + 2 H2O + NH4(+) = 6 [Fe(II)cytochrome
CC         c] + 8 H(+) + nitrite; Xref=Rhea:RHEA:13089, Rhea:RHEA-COMP:10350,
CC         Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=1.7.2.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01182};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01182};
CC       Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01182};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01182};
CC       Note=Binds 5 heme groups covalently per monomer. {ECO:0000255|HAMAP-
CC       Rule:MF_01182};
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC       {ECO:0000255|HAMAP-Rule:MF_01182}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01182}.
CC   -!- SIMILARITY: Belongs to the cytochrome c-552 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01182}.
DR   EMBL; AE004439; AAK02107.1; -; Genomic_DNA.
DR   SMR; Q9CPL4; -.
DR   PRIDE; Q9CPL4; -.
DR   EnsemblBacteria; AAK02107; AAK02107; PM0023.
DR   KEGG; pmu:PM0023; -.
DR   eggNOG; ENOG4105EAU; Bacteria.
DR   eggNOG; COG3303; LUCA.
DR   HOGENOM; HOG000278511; -.
DR   KO; K03385; -.
DR   OMA; EMVILWA; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042279; F:nitrite reductase (cytochrome, ammonia-forming) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01182; Cytochrom_C552; 1.
DR   InterPro; IPR003321; Cyt_c552.
DR   InterPro; IPR017570; Cyt_c_NO2Rdtase_formate-dep.
DR   InterPro; IPR011031; Multihaem_cyt.
DR   InterPro; IPR036280; Multihaem_cyt_sf.
DR   PANTHER; PTHR30633; PTHR30633; 1.
DR   Pfam; PF02335; Cytochrom_C552; 1.
DR   PIRSF; PIRSF000243; Cyt_c552; 1.
DR   SUPFAM; SSF48695; SSF48695; 1.
DR   TIGRFAMs; TIGR03152; cyto_c552_HCOOH; 1.
DR   PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9CPL4.
DR   SWISS-2DPAGE; Q9CPL4.
KW   Calcium; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase;
KW   Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL          1..50
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   CHAIN           51..510
FT                   /note="Cytochrome c-552"
FT                   /id="PRO_0000006580"
FT   METAL           124
FT                   /note="Iron (heme 3 axial ligand)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   METAL           156
FT                   /note="Iron (heme 1 axial ligand)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   METAL           194
FT                   /note="Iron (heme 2 axial ligand)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   METAL           243
FT                   /note="Iron (heme 3 axial ligand)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   METAL           245
FT                   /note="Calcium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   METAL           246
FT                   /note="Calcium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   METAL           291
FT                   /note="Calcium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   METAL           293
FT                   /note="Calcium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   METAL           305
FT                   /note="Iron (heme 5 axial ligand)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   METAL           316
FT                   /note="Iron (heme 4 axial ligand)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   METAL           331
FT                   /note="Iron (heme 2 axial ligand)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   METAL           348
FT                   /note="Iron (heme 5 axial ligand)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   METAL           423
FT                   /note="Iron (heme 4 axial ligand)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         152
FT                   /note="Heme 1 (covalent)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         155
FT                   /note="Heme 1 (covalent)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         190
FT                   /note="Heme 2 (covalent)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         193
FT                   /note="Heme 2 (covalent)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         239
FT                   /note="Heme 3 (covalent)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         242
FT                   /note="Heme 3 (covalent)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         246
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         294
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         312
FT                   /note="Heme 4 (covalent)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         315
FT                   /note="Heme 4 (covalent)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         344
FT                   /note="Heme 5 (covalent)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         347
FT                   /note="Heme 5 (covalent)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
SQ   SEQUENCE   510 AA;  57260 MW;  40A2695C513DBC43 CRC64;
     MVVFLFILYR QSDLKFKSMN GVIIVNTLKK RLFVATTMIW GLSVTLPVLA EYKPIEQPVE
     PANPSLKIES RNDLFKEKYP KQYQTWADTS KSTDLDSVNY EDPRVIVLWA GYAFAKDYKK
     PRGHFYAVTD VREILRTAAP MTPDAGPMPM ACWSCKSPDV PRLIAERGEA GYFGATWASG
     GSEVVNPIGC ADCHDTTSKD FAEGKPALRI ARPYVLRALE KIDHKFDTSD RTDQRAALCA
     NCHVEYYFAG DLKQVTFPWD NGITVDAMEK YYDDIGFVDW THAVSKAPML KAQHPDYETW
     MLGVHGKNGV TCIDCHMPKV QGADGKVYTD HQIGNPFNAF EHTCANCHDQ SKEKLQAMVK
     SRKTEIKDVM LRLEDQLVAA HFEAKAAWEA GATKEEMKEA LQDIRHAQWR WDYAAAGHGG
     HIHAPDVLLK VIGTGLDKSS DARTKLVRVL AKHGITDPVQ LPDISTAENA WKATGVDIEK
     ERKAKAEFLK TVVPQWDKEA REKGLLPAEK
//

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