NRFA_PECCP
ID NRFA_PECCP Reviewed; 477 AA.
AC C6DK80;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=PC1_2432;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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)-
CC [cytochrome c] + 8 H(+) + nitrite; 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;
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 c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000255|HAMAP-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; CP001657; ACT13463.1; -; Genomic_DNA.
DR AlphaFoldDB; C6DK80; -.
DR SMR; C6DK80; -.
DR STRING; 561230.PC1_2432; -.
DR EnsemblBacteria; ACT13463; ACT13463; PC1_2432.
DR KEGG; pct:PC1_2432; -.
DR eggNOG; COG3303; Bacteria.
DR HOGENOM; CLU_035040_1_0_6; -.
DR OMA; EMVILWA; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000002736; 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:0009061; P:anaerobic respiration; IEA:UniProt.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR CDD; cd00548; NrfA-like; 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 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;
KW Calcium; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase;
KW Periplasm; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT CHAIN 27..477
FT /note="Cytochrome c-552"
FT /id="PRO_5000486452"
FT BINDING 94
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 122
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 125
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 126
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 160
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 163
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 164
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 209
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 212
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 213
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 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT BINDING 275
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 282
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 285
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 286
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 301
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 314
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 317
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 318
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 393
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 477 AA; 53184 MW; C3BCBF1AD06BEDBC CRC64;
MVRISTSISY LWGMVASLFL MMPAYSADAP VSSPPAPIEA RNSVFTAQHP DQFNSWKATS
EQSERHDALA EDPYMVILWA GYPFSRDYNK PRGHAYAITD VRETLRTGAP KTAEDGPLPM
ACWSCKSPDV ARLIQQEGED GYFKGKWARG GPEITNDLGC ADCHDTASPD FAQGKPALTL
SRPYAERAME AIGKPFDQAS RFGQQSMVCG QCHVEYYFSG KDKAVKFPWD NGTKVEDMEK
YYDAISFSDW TNTLSRAPML KAQHPEYETW SVGIHGKNNV TCIDCHMPKV KNADGKLYTD
HKIGNPFDNY GETCTNCHTQ DKAAMQAVVA ERKTAIHELK LKAEEQLVHA HFEAKAAWDA
GATEAEMQPI LMDIRHAQWR WDLAVASHGI HMHAPDEGLR MLGTSLSKSA EARTKLVRLL
AQKGVTGEVK LPDISTKEKA QQAIGLNMQQ IKAEKQDFLN TVVPQWDEQA RKAGRLN
