NRFA_DESVH
ID NRFA_DESVH Reviewed; 524 AA.
AC Q72EF3; Q6ZXS8;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cytochrome c nitrite reductase subunit NrfA {ECO:0000303|PubMed:15547266, ECO:0000303|PubMed:16754983};
DE Short=cNiR subunit NrfA {ECO:0000303|PubMed:16754983};
DE EC=1.7.2.2 {ECO:0000255, ECO:0000269|PubMed:11004582, ECO:0000269|PubMed:17139260, ECO:0000269|PubMed:18597779, ECO:0000269|PubMed:25534748};
DE AltName: Full=Cytochrome c-type protein NrfA {ECO:0000305};
DE Flags: Precursor;
GN Name=nrfA {ECO:0000303|PubMed:15547266, ECO:0000312|EMBL:CAG27083.1};
GN OrderedLocusNames=DVU_0625 {ECO:0000312|EMBL:AAS95106.1};
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882 {ECO:0000312|EMBL:AAS95106.1};
RN [1] {ECO:0000312|EMBL:AAS95106.1, ECO:0000312|Proteomes:UP000002194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC {ECO:0000312|Proteomes:UP000002194};
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
RN [2] {ECO:0000312|EMBL:CAG27083.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 155-321.
RX PubMed=19712292; DOI=10.1016/j.femsec.2004.04.012;
RA Mohan S.B., Schmid M., Jetten M., Cole J.;
RT "Detection and widespread distribution of the nrfA gene encoding nitrite
RT reduction to ammonia, a short circuit in the biological nitrogen cycle that
RT competes with denitrification.";
RL FEMS Microbiol. Ecol. 49:433-443(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC {ECO:0000303|PubMed:11004582};
RX PubMed=11004582; DOI=10.1016/s0167-4838(00)00111-4;
RA Pereira I.A., LeGall J., Xavier A.V., Teixeira M.;
RT "Characterization of a heme c nitrite reductase from a non-ammonifying
RT microorganism, Desulfovibrio vulgaris Hildenborough.";
RL Biochim. Biophys. Acta 1481:119-130(2000).
RN [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15547266; DOI=10.1128/jb.186.23.7944-7950.2004;
RA Haveman S.A., Greene E.A., Stilwell C.P., Voordouw J.K., Voordouw G.;
RT "Physiological and gene expression analysis of inhibition of Desulfovibrio
RT vulgaris hildenborough by nitrite.";
RL J. Bacteriol. 186:7944-7950(2004).
RN [5]
RP CRYSTALLIZATION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC {ECO:0000303|PubMed:16754983};
RX PubMed=16754983; DOI=10.1107/s1744309106016629;
RA Rodrigues M.L., Oliveira T., Matias P.M., Martins I.C., Valente F.M.,
RA Pereira I.A., Archer M.;
RT "Crystallization and preliminary structure determination of the membrane-
RT bound complex cytochrome c nitrite reductase from Desulfovibrio vulgaris
RT Hildenborough.";
RL Acta Crystallogr. F 62:565-568(2006).
RN [6]
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, EPR SPECTROSCOPY OF THE NRFHA
RP COMPLEX, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=22519292; DOI=10.1021/jp301356m;
RA Todorovic S., Rodrigues M.L., Matos D., Pereira I.A.;
RT "Redox properties of lysine- and methionine-coordinated hemes ensure
RT downhill electron transfer in NrfH2A4 nitrite reductase.";
RL J. Phys. Chem. B 116:5637-5643(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC {ECO:0000303|PubMed:25534748};
RX PubMed=25534748; DOI=10.1021/es504484m;
RA Korte H.L., Saini A., Trotter V.V., Butland G.P., Arkin A.P., Wall J.D.;
RT "Independence of nitrate and nitrite inhibition of Desulfovibrio vulgaris
RT Hildenborough and use of nitrite as a substrate for growth.";
RL Environ. Sci. Technol. 49:924-931(2015).
RN [8] {ECO:0007744|PDB:2J7A}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 25-524 IN COMPLEX WITH CALCIUM;
RP HEME AND NRFH, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC {ECO:0000303|PubMed:17139260};
RX PubMed=17139260; DOI=10.1038/sj.emboj.7601439;
RA Rodrigues M.L., Oliveira T.F., Pereira I.A., Archer M.;
RT "X-ray structure of the membrane-bound cytochrome c quinol dehydrogenase
RT NrfH reveals novel haem coordination.";
RL EMBO J. 25:5951-5960(2006).
RN [9] {ECO:0007744|PDB:2VR0}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH CALCIUM; HEME AND
RP NRFH, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18597779; DOI=10.1016/j.jmb.2008.05.066;
RA Rodrigues M.L., Scott K.A., Sansom M.S., Pereira I.A., Archer M.;
RT "Quinol oxidation by c-type cytochromes: structural characterization of the
RT menaquinol binding site of NrfHA.";
RL J. Mol. Biol. 381:341-350(2008).
CC -!- FUNCTION: Catalytic subunit of the cytochrome c nitrite reductase
CC holocomplex NrfHA (PubMed:11004582, PubMed:25534748, PubMed:17139260,
CC PubMed:18597779). Has both nitrite and sulfite reductase activities
CC (PubMed:11004582). Catalyzes the reduction of nitrite to ammonia,
CC consuming six electrons acquired by the electron donor subunit NrfH
CC from the menaquinone pool, in an anaerobic respiratory process of
CC nitrite (PubMed:11004582, PubMed:25534748, PubMed:17139260,
CC PubMed:18597779). The other biological function of the NrfHA
CC holocomplex is to detoxify nitrite (PubMed:15547266, PubMed:25534748).
CC This function is essential for the survival of this organism as it
CC enables it to overcome inhibition by nitrite, which is produced by
CC other organisms living in the same environment (Probable).
CC {ECO:0000269|PubMed:11004582, ECO:0000269|PubMed:15547266,
CC ECO:0000269|PubMed:17139260, ECO:0000269|PubMed:18597779,
CC ECO:0000269|PubMed:25534748, ECO:0000305}.
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, ECO:0000269|PubMed:11004582,
CC ECO:0000269|PubMed:17139260, ECO:0000269|PubMed:18597779,
CC ECO:0000269|PubMed:25534748};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255, ECO:0000269|PubMed:17139260,
CC ECO:0000269|PubMed:18597779};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000255, ECO:0000269|PubMed:17139260,
CC ECO:0000269|PubMed:18597779, ECO:0000269|PubMed:22519292};
CC Note=Binds 5 heme groups per subunit (PubMed:17139260,
CC PubMed:18597779). The catalytic lysine-coordinated high spin heme 1
CC redox potential value indicates that a driving force for a downhill
CC electron transfer is ensured in the NrfH2A4 complex (PubMed:22519292).
CC {ECO:0000269|PubMed:17139260, ECO:0000269|PubMed:18597779,
CC ECO:0000269|PubMed:22519292};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=685 umol/min/mg enzyme for the nitrite reductase activity
CC {ECO:0000269|PubMed:11004582};
CC Vmax=1.0 umol/min/mg enzyme for the sulfite reductase activity
CC {ECO:0000269|PubMed:11004582};
CC Redox potential:
CC E(0) is -50 mV for the lysine-coordinated heme 1.
CC {ECO:0000269|PubMed:22519292};
CC -!- SUBUNIT: Component of the NrfHA cytochrome c nitrite reductase complex
CC composed of 4 NrfA catalytic subunits and 2 NrfH quinone-binding
CC subunits (PubMed:17139260, PubMed:18597779, PubMed:22519292). NrfA
CC homodimer interacts with NrfH (PubMed:16754983, PubMed:17139260).
CC {ECO:0000269|PubMed:16754983, ECO:0000269|PubMed:17139260,
CC ECO:0000269|PubMed:18597779, ECO:0000269|PubMed:22519292}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11004582,
CC ECO:0000269|PubMed:16754983, ECO:0000269|PubMed:17139260,
CC ECO:0000269|PubMed:18597779, ECO:0000269|PubMed:22519292}; Peripheral
CC membrane protein {ECO:0000269|PubMed:16754983,
CC ECO:0000269|PubMed:17139260, ECO:0000269|PubMed:18597779}; Periplasmic
CC side {ECO:0000269|PubMed:16754983, ECO:0000269|PubMed:17139260,
CC ECO:0000269|PubMed:18597779}.
CC -!- INDUCTION: Expression is induced in response to nitrite stress. Not
CC induced by nitrate. {ECO:0000269|PubMed:15547266}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to nitrite, but not to nitrate
CC (PubMed:15547266). Loss of anaerobical respiration of nitrite, but the
CC mutant is still able to utilize nitrite as a nitrogen source for growth
CC (PubMed:25534748). {ECO:0000269|PubMed:15547266,
CC ECO:0000269|PubMed:25534748}.
CC -!- SIMILARITY: Belongs to the cytochrome c-552 family. {ECO:0000305}.
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DR EMBL; AE017285; AAS95106.1; -; Genomic_DNA.
DR EMBL; AJ697975; CAG27083.1; -; Genomic_DNA.
DR RefSeq; WP_010937928.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_009847.1; NC_002937.3.
DR PDB; 2J7A; X-ray; 2.30 A; A/B/D/E/G/H/J/K/M/N/P/Q=25-524.
DR PDB; 2VR0; X-ray; 2.80 A; A/B/D/E=1-524.
DR PDBsum; 2J7A; -.
DR PDBsum; 2VR0; -.
DR AlphaFoldDB; Q72EF3; -.
DR SMR; Q72EF3; -.
DR STRING; 882.DVU_0625; -.
DR DrugBank; DB07918; 2-heptyl-4-hydroxyquinoline N-oxide.
DR PaxDb; Q72EF3; -.
DR EnsemblBacteria; AAS95106; AAS95106; DVU_0625.
DR KEGG; dvu:DVU_0625; -.
DR PATRIC; fig|882.5.peg.583; -.
DR eggNOG; COG3303; Bacteria.
DR HOGENOM; CLU_035040_1_0_7; -.
DR OMA; EMVILWA; -.
DR PhylomeDB; Q72EF3; -.
DR BRENDA; 1.7.7.1; 1914.
DR EvolutionaryTrace; Q72EF3; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042279; F:nitrite reductase (cytochrome, ammonia-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd00548; NrfA-like; 1.
DR InterPro; IPR003321; Cyt_c552.
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; Cell inner membrane; Cell membrane; Heme; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Signal;
KW Stress response.
FT SIGNAL 1..24
FT /evidence="ECO:0000305|PubMed:17139260"
FT CHAIN 25..524
FT /note="Cytochrome c nitrite reductase subunit NrfA"
FT /evidence="ECO:0000305|PubMed:17139260"
FT /id="PRO_5004285214"
FT REGION 29..39
FT /note="Interaction with NrfH"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0007744|PDB:2J7A"
FT REGION 221..222
FT /note="Interaction with NrfH"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0007744|PDB:2J7A"
FT REGION 318..331
FT /note="Interaction with NrfH"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0007744|PDB:2J7A"
FT REGION 351..355
FT /note="Interaction with NrfH"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0007744|PDB:2J7A"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 121
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 147
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0007744|PDB:2J7A"
FT BINDING 150
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 151
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:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 187
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0007744|PDB:2J7A"
FT BINDING 190
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:18597779,
FT ECO:0007744|PDB:2VR0"
FT BINDING 191
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 229
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 232
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0007744|PDB:2J7A"
FT BINDING 233
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 309
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 316
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 319
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0007744|PDB:2J7A"
FT BINDING 320
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 335
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 349
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 352
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 353
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT BINDING 434
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0000269|PubMed:18597779, ECO:0007744|PDB:2J7A,
FT ECO:0007744|PDB:2VR0"
FT SITE 59
FT /note="Interaction with NrfH"
FT /evidence="ECO:0000269|PubMed:17139260,
FT ECO:0007744|PDB:2J7A"
FT CONFLICT 159..160
FT /note="VK -> FP (in Ref. 2; CAG27083)"
FT /evidence="ECO:0000305"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2J7A"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2J7A"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2J7A"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:2J7A"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:2J7A"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2VR0"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:2J7A"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:2J7A"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:2J7A"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:2J7A"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:2J7A"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:2J7A"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:2J7A"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:2J7A"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2J7A"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:2J7A"
FT TURN 308..313
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:2J7A"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:2J7A"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:2J7A"
FT TURN 347..355
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 358..394
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 404..426
FT /evidence="ECO:0007829|PDB:2J7A"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 436..459
FT /evidence="ECO:0007829|PDB:2J7A"
FT TURN 460..465
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 466..469
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 473..476
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:2J7A"
FT HELIX 498..502
FT /evidence="ECO:0007829|PDB:2J7A"
SQ SEQUENCE 524 AA; 60003 MW; 7E8B228E5BEDF12F CRC64;
MNNQKTFKGL RLAALGLVAV AAFTAGCSDV STELKTPVYK TKLTAEEIRN SAFKPEFPKQ
YASYERNDET TVMTEYKGSV PFNKNDNVNP LPEGYRHAQP YLKNLWLGYP FMYEYREARG
HTYAIQDFLH IDRINRYAEK GGLPATCWNC KTPKMMEWVK ESGDGFWAKD VNEFRDKIDM
KDHTIGCATC HDPQTMELRI TSVPLTDYLV SQGKDPKKLP RNEMRALVCG QCHVEYYFNG
PTMGVNKKPV FPWAEGFDPA DMYRYYDKHG DLQVKGFEGK FADWTHPASK TPMIKAQHPE
YETWINGTHG AAGVTCADCH MSYTRSDDKK KISSHWWTSP MKDPEMRACR QCHSDKTPDY
LKSRVLFTQK RTFDLLLAAQ EVSVKAHEAV RLANEYQGAK AAGYDDLMIQ AREMVRKGQF
FWDYVSAENS VGFHNPAKAL DTLAQSQQFS QKAIDLAMEA TQYGIGKDLS GDIKTIVPPI
LKMNRKLQQD PEFMKTHKWF QYLPVLPKAD QVWDGQKRLV SAKQ
