NRFA_ECOLI
ID NRFA_ECOLI Reviewed; 478 AA.
AC P0ABK9; P32050; Q2M6N4;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cytochrome c-552 {ECO:0000303|PubMed:7934939};
DE EC=1.7.2.2 {ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941, ECO:0000269|PubMed:20629638, ECO:0000269|PubMed:9593308};
DE AltName: Full=Ammonia-forming cytochrome c nitrite reductase;
DE Short=Cytochrome c nitrite reductase {ECO:0000303|PubMed:11863430};
DE Flags: Precursor;
GN Name=nrfA; OrderedLocusNames=b4070, JW4031;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-42 AND 150-167,
RP FUNCTION, SUBCELLULAR LOCATION, COFACTOR, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=7934939; DOI=10.1111/j.1365-2958.1993.tb01255.x;
RA Darwin A., Hussain H.A., Griffiths L., Grove J., Sambongi Y., Busby S.,
RA Cole J.;
RT "Regulation and sequence of the structural gene for cytochrome c552 from
RT Escherichia coli: not a hexahaem but a 50 kDa tetrahaem nitrite
RT reductase.";
RL Mol. Microbiol. 9:1255-1265(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CHARACTERIZATION AS A CYTOCHROME C.
RX PubMed=8039676; DOI=10.1111/j.1574-6968.1994.tb06872.x;
RA Iobbi-Nivol C., Crooke H., Griffiths L., Grov J., Hussain H., Pommier J.,
RA Mejean V., Cole J.A.;
RT "A reassessment of the range of c-type cytochromes synthesized by
RT Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 119:89-94(1994).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, HEME-BINDING, COFACTOR, SUBCELLULAR LOCATION,
RP MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-126.
RC STRAIN=K12 / JCB7120;
RX PubMed=9593308; DOI=10.1046/j.1365-2958.1998.00792.x;
RA Eaves D.J., Grove J., Staudenmann W., James P., Poole R.K., White S.A.,
RA Griffiths I., Cole J.A.;
RT "Involvement of products of the nrfEFG genes in the covalent attachment of
RT haem c to a novel cysteine-lysine motif in the cytochrome c552 nitrite
RT reductase from Escherichia coli.";
RL Mol. Microbiol. 28:205-216(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CALCIUM AND HEME,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBCELLULAR
RP LOCATION, MAGNETIC CIRCULAR DICHROISM, AND EPR SPECTROSCOPY.
RX PubMed=11863430; DOI=10.1021/bi015765d;
RA Bamford V.A., Angove H.C., Seward H.E., Thomson A.J., Cole J.A., Butt J.N.,
RA Hemmings A.M., Richardson D.J.;
RT "Structure and spectroscopy of the periplasmic cytochrome c nitrite
RT reductase from Escherichia coli.";
RL Biochemistry 41:2921-2931(2002).
RN [8] {ECO:0007744|PDB:2RDZ, ECO:0007744|PDB:2RF7}
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 27-478 IN COMPLEX WITH CALCIUM
RP AND HEME, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF GLN-263.
RX PubMed=18311941; DOI=10.1021/bi702175w;
RA Clarke T.A., Kemp G.L., Van Wonderen J.H., Doyle R.M., Cole J.A.,
RA Tovell N., Cheesman M.R., Butt J.N., Richardson D.J., Hemmings A.M.;
RT "Role of a conserved glutamine residue in tuning the catalytic activity of
RT Escherichia coli cytochrome c nitrite reductase.";
RL Biochemistry 47:3789-3799(2008).
RN [9] {ECO:0007744|PDB:3L1T}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 27-478 IN COMPLEX WITH CALCIUM;
RP HEME AND HYDROGENSULFITE, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND COFACTOR.
RX PubMed=20629638; DOI=10.1042/bj20100866;
RA Kemp G.L., Clarke T.A., Marritt S.J., Lockwood C., Poock S.R.,
RA Hemmings A.M., Richardson D.J., Cheesman M.R., Butt J.N.;
RT "Kinetic and thermodynamic resolution of the interactions between sulfite
RT and the pentahaem cytochrome NrfA from Escherichia coli.";
RL Biochem. J. 431:73-80(2010).
RN [10] {ECO:0007744|PDB:3TOR}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 27-478 IN COMPLEX WITH CALCIUM
RP AND HEME, AND COFACTOR.
RX PubMed=22103542; DOI=10.1042/bst20110731;
RA Lockwood C.W., Clarke T.A., Butt J.N., Hemmings A.M., Richardson D.J.;
RT "Characterization of the active site and calcium binding in cytochrome c
RT nitrite reductases.";
RL Biochem. Soc. Trans. 39:1871-1875(2011).
CC -!- FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming six
CC electrons in the process (PubMed:9593308, PubMed:11863430,
CC PubMed:18311941, PubMed:20629638). Has very low activity toward
CC hydroxylamine (PubMed:11863430). Has even lower activity toward sulfite
CC (PubMed:20629638). Sulfite reductase activity is maximal at neutral pH
CC (By similarity). {ECO:0000250|UniProtKB:L0DSL2,
CC ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941,
CC ECO:0000269|PubMed:20629638, ECO:0000269|PubMed:9593308,
CC ECO:0000305|PubMed:7934939}.
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:11863430, ECO:0000269|PubMed:18311941,
CC ECO:0000269|PubMed:20629638, ECO:0000269|PubMed:9593308};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941,
CC ECO:0000269|PubMed:20629638, ECO:0000269|PubMed:22103542};
CC Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000269|PubMed:11863430,
CC ECO:0000269|PubMed:18311941, ECO:0000269|PubMed:20629638,
CC ECO:0000269|PubMed:22103542};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941,
CC ECO:0000269|PubMed:20629638, ECO:0000269|PubMed:22103542,
CC ECO:0000269|PubMed:7934939, ECO:0000269|PubMed:9593308};
CC Note=Binds 5 heme c groups covalently per monomer.
CC {ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941,
CC ECO:0000269|PubMed:20629638, ECO:0000269|PubMed:22103542};
CC -!- ACTIVITY REGULATION: Subject to competitive inhibition by sulfite.
CC {ECO:0000269|PubMed:20629638}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28 uM for nitrite {ECO:0000269|PubMed:11863430};
CC KM=30 uM for nitrite {ECO:0000269|PubMed:18311941};
CC KM=22 uM for nitrite {ECO:0000269|PubMed:20629638};
CC KM=70 uM for sulfite {ECO:0000269|PubMed:20629638};
CC KM=30 mM for hydroxylamine {ECO:0000269|PubMed:11863430};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC {ECO:0000305|PubMed:7934939}.
CC -!- SUBUNIT: Homodimer (PubMed:11863430, PubMed:18311941). Component of a
CC membrane-associated heterooligomeric complex (Probable).
CC {ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11863430,
CC ECO:0000269|PubMed:7934939, ECO:0000269|PubMed:9593308}.
CC -!- INDUCTION: Full induction attained in the presence of nitrite. Subject
CC to glucose and nitrate repression. {ECO:0000269|PubMed:7934939}.
CC -!- MASS SPECTROMETRY: Mass=53590; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9593308};
CC -!- SIMILARITY: Belongs to the cytochrome c-552 family. {ECO:0000305}.
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DR EMBL; X72298; CAA51048.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43164.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77040.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78072.1; -; Genomic_DNA.
DR PIR; S39590; S39590.
DR RefSeq; NP_418494.1; NC_000913.3.
DR RefSeq; WP_000196875.1; NZ_STEB01000014.1.
DR PDB; 1GU6; X-ray; 2.50 A; A/C/E/G=27-478.
DR PDB; 2RDZ; X-ray; 1.74 A; A/B/C/D=27-478.
DR PDB; 2RF7; X-ray; 2.04 A; A/B/C/D=37-477.
DR PDB; 3L1T; X-ray; 2.30 A; A/B/C/D=27-478.
DR PDB; 3TOR; X-ray; 2.00 A; A/B/C/D=27-478.
DR PDB; 4WJY; X-ray; 2.15 A; A/B=27-478.
DR PDBsum; 1GU6; -.
DR PDBsum; 2RDZ; -.
DR PDBsum; 2RF7; -.
DR PDBsum; 3L1T; -.
DR PDBsum; 3TOR; -.
DR PDBsum; 4WJY; -.
DR AlphaFoldDB; P0ABK9; -.
DR SMR; P0ABK9; -.
DR BioGRID; 4259405; 27.
DR DIP; DIP-36021N; -.
DR IntAct; P0ABK9; 3.
DR STRING; 511145.b4070; -.
DR DrugBank; DB03317; Ferroheme C.
DR jPOST; P0ABK9; -.
DR PaxDb; P0ABK9; -.
DR PRIDE; P0ABK9; -.
DR EnsemblBacteria; AAC77040; AAC77040; b4070.
DR EnsemblBacteria; BAE78072; BAE78072; BAE78072.
DR GeneID; 66672014; -.
DR GeneID; 948571; -.
DR KEGG; ecj:JW4031; -.
DR KEGG; eco:b4070; -.
DR PATRIC; fig|1411691.4.peg.2634; -.
DR EchoBASE; EB1729; -.
DR eggNOG; COG3303; Bacteria.
DR HOGENOM; CLU_035040_1_0_6; -.
DR InParanoid; P0ABK9; -.
DR OMA; EMVILWA; -.
DR PhylomeDB; P0ABK9; -.
DR BioCyc; EcoCyc:CYTOCHROMEC552-MON; -.
DR BioCyc; MetaCyc:CYTOCHROMEC552-MON; -.
DR BRENDA; 1.7.2.2; 2026.
DR SABIO-RK; P0ABK9; -.
DR UniPathway; UPA00653; -.
DR EvolutionaryTrace; P0ABK9; -.
DR PRO; PR:P0ABK9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016966; F:nitric oxide reductase activity; IDA:CACAO.
DR GO; GO:0042279; F:nitrite reductase (cytochrome, ammonia-forming) activity; IDA:EcoCyc.
DR GO; GO:0019645; P:anaerobic electron transport chain; IMP:EcoCyc.
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 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..26
FT /evidence="ECO:0000269|PubMed:7934939"
FT CHAIN 27..478
FT /note="Cytochrome c-552"
FT /id="PRO_0000006578"
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:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 122
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 125
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 126
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:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 160
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 163
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
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:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 209
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 212
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
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:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:3L1T, ECO:0007744|PDB:3TOR"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000305"
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:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 282
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 285
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7"
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:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
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:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 314
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT BINDING 317
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7"
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:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
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:0007744|PDB:1GU6, ECO:0007744|PDB:2RDZ,
FT ECO:0007744|PDB:2RF7, ECO:0007744|PDB:3L1T,
FT ECO:0007744|PDB:3TOR"
FT MUTAGEN 126
FT /note="K->H,I,L: Almost complete loss of nitrite reductase
FT activity."
FT /evidence="ECO:0000269|PubMed:9593308"
FT MUTAGEN 263
FT /note="Q->E: Increases affinity for nitrite without
FT changing Vmax."
FT /evidence="ECO:0000269|PubMed:18311941"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:2RDZ"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:2RDZ"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2RDZ"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:2RDZ"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:2RDZ"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:2RDZ"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:2RDZ"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:2RDZ"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2RDZ"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:2RDZ"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:2RDZ"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:2RDZ"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:2RDZ"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:2RDZ"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 306..312
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 322..359
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 364..385
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 390..393
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 395..422
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 437..443
FT /evidence="ECO:0007829|PDB:2RDZ"
FT HELIX 448..472
FT /evidence="ECO:0007829|PDB:2RDZ"
SQ SEQUENCE 478 AA; 53703 MW; F965E986412A0456 CRC64;
MTRIKINARR IFSLLIPFFF FTSVHAEQTA APAKPVTVEA KNETFAPQHP DQYLSWKATS
EQSERVDALA EDPRLVILWA GYPFSRDYNK PRGHAFAVTD VRETLRTGAP KNAEDGPLPM
ACWSCKSPDV ARLIQKDGED GYFHGKWARG GPEIVNNLGC ADCHNTASPE FAKGKPELTL
SRPYAARAME AIGKPFEKAG RFDQQSMVCG QCHVEYYFDG KNKAVKFPWD DGMKVENMEQ
YYDKIAFSDW TNSLSKTPML KAQHPEYETW TAGIHGKNNV TCIDCHMPKV QNAEGKLYTD
HKIGNPFDNF AQTCANCHTQ DKAALQKVVA ERKQSINDLK IKVEDQLVHA HFEAKAALDA
GATEAEMKPI QDDIRHAQWR WDLAIASHGI HMHAPEEGLR MLGTAMDKAA DARTKLARLL
ATKGITHEIQ IPDISTKEKA QQAIGLNMEQ IKAEKQDFIK TVIPQWEEQA RKNGLLSQ
