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NRFA_PARD8
ID   NRFA_PARD8              Reviewed;         494 AA.
AC   A6L890;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=BDI_0109;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR41904.1; -; Genomic_DNA.
DR   RefSeq; WP_011965891.1; NC_009615.1.
DR   AlphaFoldDB; A6L890; -.
DR   SMR; A6L890; -.
DR   STRING; 435591.BDI_0109; -.
DR   EnsemblBacteria; ABR41904; ABR41904; BDI_0109.
DR   KEGG; pdi:BDI_0109; -.
DR   PATRIC; fig|435591.13.peg.105; -.
DR   eggNOG; COG3303; Bacteria.
DR   HOGENOM; CLU_035040_1_0_10; -.
DR   OMA; EMVILWA; -.
DR   OrthoDB; 738283at2; -.
DR   BioCyc; PDIS435591:G1G5A-109-MON; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000000566; 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   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   PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE   3: Inferred from homology;
KW   Calcium; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase;
KW   Periplasm; Reference proteome; Repeat; Signal; Transport.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   CHAIN           32..494
FT                   /note="Cytochrome c-552"
FT                   /id="PRO_1000065804"
FT   BINDING         116
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         144
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         147
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         148
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         182
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         185
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         186
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         224
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         227
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         228
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         230
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         231
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         276
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         278
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         290
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         297
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         300
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         301
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         315
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         328
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         331
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         332
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         407
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   494 AA;  56145 MW;  58ECCCF0E077EF53 CRC64;
     MEKKLKSWQG WLLFGGTMVV VFVLGMIAAS VNERHAEVTS VMNNKKTEIT GIEARNDKFE
     SNYPREYQTW EATADTSFKS LYNGNQAVDV LEARPEMVIL WAGYAFSKDY STPRGHMHAI
     EDMRNTLRVG APMTENEGPQ PATCWTCKSP DVPRMMQAMG VDNFYKGKWA SLGKEIVNPI
     GCADCHEPEN MNLHISRPAL IEAFQRQGKD ITKATQQEMR SLVCAQCHVE YYFKGDGKYL
     TFPWDKGSTV EDMEAYYDEA GFADYTHKLS RAPILKAQHP DYEISQMGIH AQRGVSCADC
     HMPYKSEGGV KYSDHHIQSP LAMIDRTCQV CHRESEETLR NNVYERQNKA NEMRNRLETE
     LAKAHVEAKF AWDKGATEDQ MKDVLKLIRQ AQWRWDFGVA SHGGAFHAPQ EIQRILGNGL
     DKAMQARLAT AKVLAKLGYT DDVPMPDFST KEKAQQYIGL DMAAERTAKE KFLNTIVPQW
     MKEAQENNRL AKNI
 
 
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