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NRFA_HAEI8
ID   NRFA_HAEI8              Reviewed;         538 AA.
AC   Q4QLL8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=NTHI1230;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP;
RX   PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT   influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX88079.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4QLL8; -.
DR   SMR; Q4QLL8; -.
DR   EnsemblBacteria; AAX88079; AAX88079; NTHI1230.
DR   KEGG; hit:NTHI1230; -.
DR   HOGENOM; CLU_035040_1_0_6; -.
DR   OMA; EMVILWA; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000002525; 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   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..55
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   CHAIN           56..538
FT                   /note="Cytochrome c-552"
FT                   /id="PRO_0000268967"
FT   BINDING         133
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         161
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         164
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         165
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         199
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         202
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         203
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         264
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         267
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         268
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         270
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         271
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         316
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         318
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT   BINDING         330
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         337
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         340
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         341
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         356
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         369
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         372
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         373
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         448
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   538 AA;  60367 MW;  6BB030F62F289E76 CRC64;
     MKIYLRFVWI LIIILNFLLN LFITTNGVII VNAFKKSLIV AASFASLSLF NSATAELVYK
     PLEQPVEPAK PDLKIESVNE KFAEKYPNQY NSWRSTANGD GENIIYADEE NPRLIVLWGG
     YAFAKEYNAP RGHFYAVTDV RNILRTGAPK TANDGPQAMA CWTCKGPDVP RLIAEWGEKD
     YFNAKWAKGG PEIVNSIGCA DCHDTTSKDF AEGKPALRIA RPHVLRALDA LEKATAEKDK
     AEGRPHNNLS FNTAARTEKR AEICANCHVE YYFAGDIKQV TFPWDNGQTA DDIEKYYDDI
     GFTDWTHSLS KAPMLKAQHP DFEIWSLGMH GKNGVTCVDC HMPKVQGADG KVYTDHQIQN
     PFDAFDHTCA NCHDQSKEKL RDIVTSRKKE VKDVMGRLED QVVKSHFEAK AAWDAGATKE
     EMEAALMDIR HAQWRWDYTA ASHGGHMHAP EVVLRVLASG LDKVADARTK LAVILTKHGV
     KTPVQIPDIS TADKAWKVMG IDIEKERKAK EEFLKTVVPQ WEQQAREKGL LVDPPAQK
 
 
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