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   18-JUN-2025, entry version 150.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; 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] + NH4(+) + 2 H2O = 6 Fe(II)-
CC         [cytochrome c] + nitrite + 8 H(+); Xref=Rhea:RHEA:13089, Rhea:RHEA-
CC         COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01182};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01182};
CC       Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01182};
CC   -!- COFACTOR:
CC       Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01182};
CC       Note=Binds 5 heme c 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}.
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DR   EMBL; AE004439; AAK02107.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9CPL4; -.
DR   SMR; Q9CPL4; -.
DR   STRING; 272843.PM0023; -.
DR   EnsemblBacteria; AAK02107; AAK02107; PM0023.
DR   KEGG; pmu:PM0023; -.
DR   HOGENOM; CLU_035040_1_0_6; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
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:0019645; P:anaerobic electron transport chain; IEA:TreeGrafter.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd00548; NrfA-like; 1.
DR   FunFam; 1.10.1130.10:FF:000002; Cytochrome c-552; 1.
DR   FunFam; 1.20.140.10:FF:000014; Cytochrome c-552; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   Gene3D; 1.10.1130.10; Flavocytochrome C3, Chain A; 1.
DR   HAMAP; MF_01182; Cytochrom_C552; 1.
DR   InterPro; IPR003321; Cyt_c552.
DR   InterPro; IPR017570; Cyt_c_NO2Rdtase_formate-dep.
DR   InterPro; IPR036280; Multihaem_cyt_sf.
DR   NCBIfam; TIGR03152; cyto_c552_HCOOH; 1.
DR   NCBIfam; NF008339; PRK11125.1; 1.
DR   PANTHER; PTHR30633:SF0; CYTOCHROME C-552; 1.
DR   PANTHER; PTHR30633; CYTOCHROME C-552 RESPIRATORY NITRITE REDUCTASE; 1.
DR   Pfam; PF02335; Cytochrom_C552; 1.
DR   PIRSF; PIRSF000243; Cyt_c552; 1.
DR   SUPFAM; SSF48695; Multiheme cytochromes; 1.
DR   PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE   3: Inferred from homology;
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   BINDING         124
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         152
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         155
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         156
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         190
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         193
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         194
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         239
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         242
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         243
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         245
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         246
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         291
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         293
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         305
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="5"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         312
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="4"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         315
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="4"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         316
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="4"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         331
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         344
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="5"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         347
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="5"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         348
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="5"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         423
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="4"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
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
//