NRFA_ALIB4
ID NRFA_ALIB4 Reviewed; 496 AA.
AC A8ERP8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Abu_0347;
OS Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Aliarcobacter.
OX NCBI_TaxID=367737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM4018;
RX PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA Rogosin A., Stanker L.H., Mandrell R.E.;
RT "The complete genome sequence and analysis of the Epsilonproteobacterium
RT Arcobacter butzleri.";
RL PLoS ONE 2:E1358-E1358(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; CP000361; ABV66622.1; -; Genomic_DNA.
DR RefSeq; WP_012012181.1; NC_009850.1.
DR AlphaFoldDB; A8ERP8; -.
DR SMR; A8ERP8; -.
DR STRING; 367737.Abu_0347; -.
DR EnsemblBacteria; ABV66622; ABV66622; Abu_0347.
DR KEGG; abu:Abu_0347; -.
DR eggNOG; COG3303; Bacteria.
DR HOGENOM; CLU_035040_1_0_7; -.
DR OMA; MHAPDVM; -.
DR OrthoDB; 738283at2; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000001136; 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; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT CHAIN 24..496
FT /note="Cytochrome c-552"
FT /id="PRO_1000085447"
FT BINDING 100
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 128
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 131
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 132
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 166
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 169
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 170
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 210
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 /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT BINDING 214
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 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT BINDING 269
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 272
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01182"
FT BINDING 283
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 290
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 293
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 294
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 308
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 321
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 324
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 325
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 400
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 496 AA; 56273 MW; DE03F5334191555F CRC64;
MKKYKFLFAI SIIAIGLMTV LLASINEKKE EKENLLSVPK IEKWETKNEE FRKFYPREFD
SWKQTKNSDQ IDDMLKLHPE MVVLWAGYAF SKDYNAPRGH FYAIDDVSNS LRTGAPTDKE
SGPLPSACWT CKSPDVPRIM HEQGNNEYFT GKWAKYGADI VNPIGCVDCH NPETMELQVG
RSYLNDALKA EGKSPTLATA TQQDMRTLVC AQCHVEYYFK KTPLENGKTA MAVTLPWANG
TTVEDMEKYY DTIEFSDWVH QVSKTPMIKA QHPEYETWKT GAHGRNNVSC ADCHMPYTQE
GGIKYTDHKI GNPLENMDKT CMNCHRVSEK SLLANIQDKK ARKDDLNQKA MEQIVAAHLE
AGKAWEVGAT PEEMKDILTD IRHAQWRWDF AAASHSAFFH APEETLKTLG TAIEKAGNAR
IKLAKVLAKH GVTDYKAPTI TDKKQAQELI GLPMGKLIEE KKQFTNGLLK DWKNEAEQKG
LYNPKSREGV ETKTSY
