NRFA_WOLSU
ID NRFA_WOLSU Reviewed; 507 AA.
AC Q9S1E5;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cytochrome c-552;
DE EC=1.7.2.2 {ECO:0000269|PubMed:18201106};
DE AltName: Full=Ammonia-forming cytochrome c nitrite reductase;
DE Short=Cytochrome c nitrite reductase;
DE Flags: Precursor;
GN Name=nrfA; OrderedLocusNames=WS0969;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-30, FUNCTION,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=10672190; DOI=10.1046/j.1365-2958.2000.01742.x;
RA Simon J., Gross R., Einsle O., Kroneck P.M.H., Kroeger A., Klimmek O.;
RT "A NapC/NirT-type cytochrome c (NrfH) is the mediator between the quinone
RT pool and the cytochrome c nitrite reductase of Wolinella succinogenes.";
RL Mol. Microbiol. 35:686-696(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
RN [3]
RP SUBUNIT.
RX PubMed=11807271; DOI=10.1107/s090744490102039x;
RA Einsle O., Stach P., Messerschmidt A., Klimmek O., Simon J., Kroeger A.,
RA Kroneck P.M.;
RT "Crystallization and preliminary X-ray analysis of the membrane-bound
RT cytochrome c nitrite reductase complex (NrfHA) from Wolinella
RT succinogenes.";
RL Acta Crystallogr. D 58:341-342(2002).
RN [4] {ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8, ECO:0007744|PDB:1FS9}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 23-507 IN COMPLEX WITH CALCIUM
RP AND HEME, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10984487; DOI=10.1074/jbc.m006188200;
RA Einsle O., Stach P., Messerschmidt A., Simon J., Kroeger A., Huber R.,
RA Kroneck P.M.H.;
RT "Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at
RT 1.6 A resolution, inhibitor binding, and heme-packing motifs.";
RL J. Biol. Chem. 275:39608-39616(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 23-507 IN COMPLEX WITH NITRITE;
RP CALCIUM AND HEME, SUBUNIT, SUBCELLULAR LOCATION, AND COFACTOR.
RX PubMed=12296741; DOI=10.1021/ja0206487;
RA Einsle O., Messerschmidt A., Huber R., Kroneck P.M., Neese F.;
RT "Mechanism of the six-electron reduction of nitrite to ammonia by
RT cytochrome c nitrite reductase.";
RL J. Am. Chem. Soc. 124:11737-11745(2002).
RN [6] {ECO:0007744|PDB:3BNF, ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH, ECO:0007744|PDB:3BNJ}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 23-507 IN COMPLEX WITH CALCIUM;
RP HEME AND HYDROGENSULFITE, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP TYR-218.
RX PubMed=18201106; DOI=10.1021/bi7021415;
RA Lukat P., Rudolf M., Stach P., Messerschmidt A., Kroneck P.M., Simon J.,
RA Einsle O.;
RT "Binding and reduction of sulfite by cytochrome c nitrite reductase.";
RL Biochemistry 47:2080-2086(2008).
CC -!- FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming six
CC electrons in the process. Has very low activity toward hydroxylamine,
CC and even lower activity toward sulfite. Sulfite reductase activity is
CC maximal at neutral pH. {ECO:0000269|PubMed:10672190,
CC ECO:0000269|PubMed:18201106}.
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:0000269|PubMed:18201106};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10984487, ECO:0000269|PubMed:12296741,
CC ECO:0000269|PubMed:18201106};
CC Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000269|PubMed:10984487,
CC ECO:0000269|PubMed:12296741, ECO:0000269|PubMed:18201106};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:10984487, ECO:0000269|PubMed:12296741,
CC ECO:0000269|PubMed:18201106};
CC Note=Binds 5 heme c groups covalently per monomer.
CC {ECO:0000269|PubMed:10984487, ECO:0000269|PubMed:12296741,
CC ECO:0000269|PubMed:18201106};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC -!- SUBUNIT: Homodimer (PubMed:10984487, PubMed:12296741). Interacts with
CC NrfH (PubMed:10672190). May form a heterotetramer with NrfH
CC (PubMed:11807271). {ECO:0000269|PubMed:10672190,
CC ECO:0000269|PubMed:10984487, ECO:0000269|PubMed:12296741,
CC ECO:0000305|PubMed:11807271}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10672190,
CC ECO:0000305|PubMed:10984487, ECO:0000305|PubMed:12296741}.
CC -!- SIMILARITY: Belongs to the cytochrome c-552 family. {ECO:0000305}.
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DR EMBL; AJ245540; CAB53160.1; -; Genomic_DNA.
DR EMBL; BX571659; CAE10072.1; -; Genomic_DNA.
DR RefSeq; WP_011138866.1; NC_005090.1.
DR PDB; 1FS7; X-ray; 1.60 A; A=23-507.
DR PDB; 1FS8; X-ray; 1.60 A; A=23-507.
DR PDB; 1FS9; X-ray; 2.00 A; A=1-507.
DR PDB; 2E80; X-ray; 1.60 A; A=23-507.
DR PDB; 2E81; X-ray; 2.00 A; A=23-507.
DR PDB; 3BNF; X-ray; 1.70 A; A=23-507.
DR PDB; 3BNG; X-ray; 1.50 A; A=23-507.
DR PDB; 3BNH; X-ray; 1.75 A; A=23-507.
DR PDB; 3BNJ; X-ray; 1.30 A; A=23-507.
DR PDBsum; 1FS7; -.
DR PDBsum; 1FS8; -.
DR PDBsum; 1FS9; -.
DR PDBsum; 2E80; -.
DR PDBsum; 2E81; -.
DR PDBsum; 3BNF; -.
DR PDBsum; 3BNG; -.
DR PDBsum; 3BNH; -.
DR PDBsum; 3BNJ; -.
DR AlphaFoldDB; Q9S1E5; -.
DR SMR; Q9S1E5; -.
DR STRING; 273121.WS0969; -.
DR EnsemblBacteria; CAE10072; CAE10072; WS0969.
DR KEGG; wsu:WS0969; -.
DR eggNOG; COG3303; Bacteria.
DR HOGENOM; CLU_035040_1_0_7; -.
DR OMA; MHAPDVM; -.
DR OrthoDB; 738283at2; -.
DR BRENDA; 1.7.2.2; 6642.
DR UniPathway; UPA00653; -.
DR EvolutionaryTrace; Q9S1E5; -.
DR Proteomes; UP000000422; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:UniProtKB.
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 GO; GO:0006807; P:nitrogen compound metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Electron transport; Heme;
KW Iron; Metal-binding; Oxidoreductase; Periplasm; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:10672190"
FT CHAIN 23..507
FT /note="Cytochrome c-552"
FT /id="PRO_0000006584"
FT BINDING 102
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:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 130
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 133
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 134
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 168
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 171
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 172
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:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 211
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 214
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 215
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:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000305, ECO:0007744|PDB:3BNF"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000305, ECO:0007744|PDB:3BNF"
FT BINDING 288
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:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 295
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 298
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 299
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:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 313
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:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 326
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 329
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
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:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT BINDING 405
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:0007744|PDB:1FS7, ECO:0007744|PDB:1FS8,
FT ECO:0007744|PDB:1FS9, ECO:0007744|PDB:2E80,
FT ECO:0007744|PDB:2E81, ECO:0007744|PDB:3BNF,
FT ECO:0007744|PDB:3BNG, ECO:0007744|PDB:3BNH,
FT ECO:0007744|PDB:3BNJ"
FT MUTAGEN 218
FT /note="Y->F: Reduces nitrite reductase activity by over
FT 99%, but does not decrease the low sulfite reductase
FT activity."
FT /evidence="ECO:0000269|PubMed:18201106"
FT CONFLICT 45
FT /note="E -> K (in Ref. 1; CAB53160)"
FT /evidence="ECO:0000305"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:3BNJ"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:3BNJ"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:3BNJ"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3BNJ"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:3BNJ"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:1FS7"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:3BNJ"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:3BNJ"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:3BNJ"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:3BNJ"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:3BNJ"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:3BNJ"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:3BNJ"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:3BNJ"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 279..283
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:3BNJ"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:3BNJ"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:3BNJ"
FT TURN 326..329
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 334..372
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 376..397
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 402..405
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 407..434
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 448..454
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 459..471
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 473..483
FT /evidence="ECO:0007829|PDB:3BNJ"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:3BNJ"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:3BNJ"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:1FS8"
SQ SEQUENCE 507 AA; 57511 MW; D5CE7E841E3E7AB3 CRC64;
MTKFKLLLAG SLVAIVSMGL LASNINEREK ERVALNKTAH SQGIEGKAMS EEWARYYPRQ
FDSWKKTKES DNITDMLKEK PALVVAWAGY PFSKDYNAPR GHYYALQDNI NTLRTGAPVD
GKTGPLPSAC WTCKSPDVPR IIEQDGELEY FTGKWAKYGD EIVNTIGCYN CHDDKSAELK
SKVPYLDRGL SAAGFKTFAE STHQEKRSLV CAQCHVEYYF KKTEWKDDKG VDKTAMVVTL
PWSKGISTEQ MEAYYDEINF ADWTHGISKT PMLKAQHPDW ELYKTGIHGQ KGVSCADCHM
PYTQEGAVKY SDHKVGNPLD NMDKSCMNCH RESEQKLKDI VKQKFERKEF LQDIAFDNIG
KAHLETGKAM ELGATDAELK EIRTHIRHAQ WRADMAIAGH GSFFHAPEEV LRLLASGNEE
AQKARIKLVK VLAKYGAIDY VAPDFETKEK AQKLAKVDME AFIAEKLKFK QTLEQEWKKQ
AIAKGRLNPE SLKGVDEKSS YYDKTKK
