NIR_THIND
ID NIR_THIND Reviewed; 553 AA.
AC L0DSL2; Q5F2I3;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Cytochrome c-552;
DE EC=1.7.2.2 {ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:22281743};
DE AltName: Full=Cytochrome c nitrite reductase {ECO:0000303|PubMed:16500161, ECO:0000303|PubMed:19393666};
DE AltName: Full=TvNiR {ECO:0000303|PubMed:16500161};
DE Flags: Precursor;
GN Name=nir {ECO:0000312|EMBL:AGA31970.1};
GN OrderedLocusNames=TVNIR_0259 {ECO:0000312|EMBL:AGA31970.1};
OS Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=1255043 {ECO:0000312|EMBL:AGA31970.1};
RN [1] {ECO:0000312|EMBL:CAI56199.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-44, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP ACTIVITY REGULATION.
RC STRAIN=DSM 14787 / UNIQEM 213 / ALEN2 {ECO:0000303|PubMed:16500161};
RX PubMed=16500161; DOI=10.1016/j.bbapap.2005.12.021;
RA Tikhonova T.V., Slutsky A., Antipov A.N., Boyko K.M., Polyakov K.M.,
RA Sorokin D.Y., Zvyagilskaya R.A., Popov V.O.;
RT "Molecular and catalytic properties of a novel cytochrome c nitrite
RT reductase from nitrate-reducing haloalkaliphilic sulfur-oxidizing bacterium
RT Thioalkalivibrio nitratireducens.";
RL Biochim. Biophys. Acta 1764:715-723(2006).
RN [2] {ECO:0000312|Proteomes:UP000010809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14787 / UNIQEM 213 / ALEN2 {ECO:0000312|Proteomes:UP000010809};
RA Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., Sorokin D.Y.,
RA Ravin N.V., Popov V.O.;
RT "Complete sequence of Thioalkalivibrio nitratireducens.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:2OT4, ECO:0007744|PDB:2ZO5, ECO:0007744|PDB:3D1I}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 29-553 IN COMPLEXES WITH CALCIUM;
RP AZIDE; NITRITE AND HEME, COFACTOR, SUBUNIT, AND CROSS-LINK.
RC STRAIN=DSM 14787 / UNIQEM 213 / ALEN2 {ECO:0000303|PubMed:19393666};
RX PubMed=19393666; DOI=10.1016/j.jmb.2009.04.037;
RA Polyakov K.M., Boyko K.M., Tikhonova T.V., Slutsky A., Antipov A.N.,
RA Zvyagilskaya R.A., Popov A.N., Bourenkov G.P., Lamzin V.S., Popov V.O.;
RT "High-resolution structural analysis of a novel octaheme cytochrome c
RT nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio
RT nitratireducens.";
RL J. Mol. Biol. 389:846-862(2009).
RN [4] {ECO:0007744|PDB:3FO3, ECO:0007744|PDB:3MMO}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 29-553 IN COMPLEXES WITH CALCIUM;
RP SULFITE; CYANIDE AND HEME, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=DSM 14787 / UNIQEM 213 / ALEN2 {ECO:0000303|PubMed:20944237};
RX PubMed=20944237; DOI=10.1107/s0907444910031665;
RA Trofimov A.A., Polyakov K.M., Boyko K.M., Tikhonova T.V., Safonova T.N.,
RA Tikhonov A.V., Popov A.N., Popov V.O.;
RT "Structures of complexes of octahaem cytochrome c nitrite reductase from
RT Thioalkalivibrio nitratireducens with sulfite and cyanide.";
RL Acta Crystallogr. D 66:1043-1047(2010).
RN [5] {ECO:0007744|PDB:3LG1, ECO:0007744|PDB:3LGQ, ECO:0007744|PDB:3RKH}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 33-551 IN COMPLEXES WITH SULFITE;
RP HYDROXYLAMINE; CALCIUM AND HEME, CATALYTIC ACTIVITY, FUNCTION, COFACTOR,
RP CROSS-LINK, AND SUBUNIT.
RC STRAIN=DSM 14787 / UNIQEM 213 / ALEN2 {ECO:0000303|PubMed:22281743};
RX PubMed=22281743; DOI=10.1107/s0907444911052632;
RA Trofimov A.A., Polyakov K.M., Tikhonova T.V., Tikhonov A.V., Safonova T.N.,
RA Boyko K.M., Dorovatovskii P.V., Popov V.O.;
RT "Covalent modifications of the catalytic tyrosine in octahaem cytochrome c
RT nitrite reductase and their effect on the enzyme activity.";
RL Acta Crystallogr. D 68:144-153(2012).
CC -!- FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming six
CC electrons in the process (PubMed:16500161, PubMed:22281743). Has very
CC low activity toward hydroxylamine (PubMed:16500161). Has even lower
CC activity toward sulfite (PubMed:16500161, PubMed:22281743). Sulfite
CC reductase activity is maximal at neutral pH (PubMed:20944237).
CC {ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:20944237,
CC ECO:0000269|PubMed:22281743}.
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:16500161, ECO:0000269|PubMed:22281743};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:19393666,
CC ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743};
CC Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000269|PubMed:16500161,
CC ECO:0000269|PubMed:19393666, ECO:0000269|PubMed:20944237,
CC ECO:0000269|PubMed:22281743};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:19393666,
CC ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743};
CC Note=Binds 8 heme groups covalently per monomer.
CC {ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:19393666,
CC ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743};
CC -!- ACTIVITY REGULATION: Inhibited by azide and cyanide. Subject to
CC competitive inhibition by sulfite. {ECO:0000269|PubMed:16500161}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16700 uM for nitrite {ECO:0000269|PubMed:16500161};
CC KM=16400 uM for hydroxylamine {ECO:0000269|PubMed:16500161};
CC Vmax=4080 umol/min/mg enzyme toward nitrite
CC {ECO:0000269|PubMed:16500161};
CC Vmax=45 umol/min/mg enzyme toward hydroxylamine
CC {ECO:0000269|PubMed:16500161};
CC pH dependence:
CC Optimum pH is 7-10 for nitrite reduction, and the optimum pH is 7 for
CC sulfite reduction with only 20% residual activity at pH 7.8.
CC {ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:20944237};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.
CC {ECO:0000269|PubMed:16500161};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000269|PubMed:16500161,
CC ECO:0000269|PubMed:19393666, ECO:0000305|PubMed:20944237,
CC ECO:0000305|PubMed:22281743}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: The thioether cross-link between Tyr-331 and Cys-333 may play a
CC structural role in the active site cavity (PubMed:19393666). Besides,
CC it may lower the pKa of the Tyr hydroxyl group (PubMed:19393666). An
CC additional covalent bond between Tyr-331 and Gln-388 has been observed
CC in some protein crystals, but this may be an artifact that is due to
CC the formation of tyrosyl radicals when the protein is exposed to oxygen
CC (PubMed:22281743). {ECO:0000269|PubMed:19393666,
CC ECO:0000269|PubMed:22281743}.
CC -!- SIMILARITY: Belongs to the cytochrome c-552 family. {ECO:0000305}.
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DR EMBL; AJ880678; CAI56199.2; -; Genomic_DNA.
DR EMBL; CP003989; AGA31970.1; -; Genomic_DNA.
DR RefSeq; WP_015257125.1; NC_019902.2.
DR PDB; 2OT4; X-ray; 1.50 A; A/B=29-553.
DR PDB; 2ZO5; X-ray; 1.70 A; A/B=29-553.
DR PDB; 3D1I; X-ray; 1.80 A; A/B=29-553.
DR PDB; 3F29; X-ray; 2.00 A; A/B=29-553.
DR PDB; 3FO3; X-ray; 1.40 A; A/B=29-553.
DR PDB; 3GM6; X-ray; 1.80 A; A/B=29-553.
DR PDB; 3LG1; X-ray; 1.95 A; A/B=29-553.
DR PDB; 3LGQ; X-ray; 1.80 A; A/B=29-553.
DR PDB; 3MMO; X-ray; 1.55 A; A/B=29-553.
DR PDB; 3OWM; X-ray; 1.65 A; A/B=33-551.
DR PDB; 3RKH; X-ray; 1.83 A; A/B=33-551.
DR PDB; 3S7W; X-ray; 1.79 A; A/B=33-551.
DR PDB; 3SCE; X-ray; 1.45 A; A/B=33-551.
DR PDB; 3UU9; X-ray; 2.20 A; A/B=33-552.
DR PDB; 4L38; X-ray; 1.80 A; A/B=33-551.
DR PDB; 4L3X; X-ray; 1.85 A; A/B=33-551.
DR PDB; 4L3Y; X-ray; 1.95 A; A/B=33-551.
DR PDB; 4L3Z; X-ray; 1.85 A; A/B=33-551.
DR PDB; 4Q0T; X-ray; 1.70 A; A/B=30-553.
DR PDB; 4Q17; X-ray; 1.75 A; A/B=29-553.
DR PDB; 4Q1O; X-ray; 1.75 A; A/B=29-553.
DR PDB; 4Q4U; X-ray; 1.62 A; A/B=33-553.
DR PDB; 4Q5B; X-ray; 1.80 A; A/B=33-553.
DR PDB; 4Q5C; X-ray; 1.62 A; A/B=33-553.
DR PDBsum; 2OT4; -.
DR PDBsum; 2ZO5; -.
DR PDBsum; 3D1I; -.
DR PDBsum; 3F29; -.
DR PDBsum; 3FO3; -.
DR PDBsum; 3GM6; -.
DR PDBsum; 3LG1; -.
DR PDBsum; 3LGQ; -.
DR PDBsum; 3MMO; -.
DR PDBsum; 3OWM; -.
DR PDBsum; 3RKH; -.
DR PDBsum; 3S7W; -.
DR PDBsum; 3SCE; -.
DR PDBsum; 3UU9; -.
DR PDBsum; 4L38; -.
DR PDBsum; 4L3X; -.
DR PDBsum; 4L3Y; -.
DR PDBsum; 4L3Z; -.
DR PDBsum; 4Q0T; -.
DR PDBsum; 4Q17; -.
DR PDBsum; 4Q1O; -.
DR PDBsum; 4Q4U; -.
DR PDBsum; 4Q5B; -.
DR PDBsum; 4Q5C; -.
DR AlphaFoldDB; L0DSL2; -.
DR SASBDB; L0DSL2; -.
DR SMR; L0DSL2; -.
DR STRING; 1255043.TVNIR_0259; -.
DR DrugBank; DB02580; Pentaglyme.
DR PRIDE; L0DSL2; -.
DR EnsemblBacteria; AGA31970; AGA31970; TVNIR_0259.
DR KEGG; tni:TVNIR_0259; -.
DR PATRIC; fig|1255043.3.peg.260; -.
DR eggNOG; COG3303; Bacteria.
DR HOGENOM; CLU_510704_0_0_6; -.
DR BRENDA; 1.7.2.2; 9096.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000010809; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0042279; F:nitrite reductase (cytochrome, ammonia-forming) activity; IDA:UniProtKB.
DR GO; GO:0097164; P:ammonium ion metabolic process; IDA:UniProtKB.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
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 SUPFAM; SSF48695; SSF48695; 2.
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 Thioether bond; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:16500161"
FT CHAIN 29..553
FT /note="Cytochrome c-552"
FT /id="PRO_5001089214"
FT BINDING 42
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 45
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 46
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:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 58
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:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 63
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 66
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 67
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:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 72
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:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 94
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 97
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 98
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:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 147
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:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 212
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 215
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 216
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="6"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 255
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 258
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 259
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:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743"
FT BINDING 262
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:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 324
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 327
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 328
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:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 400
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 407
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 410
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 411
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 426
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:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 439
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 442
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 443
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT BINDING 519
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743,
FT ECO:0007744|PDB:4L38, ECO:0007744|PDB:4L3X,
FT ECO:0007744|PDB:4L3Y"
FT CROSSLNK 331..333
FT /note="3'-(S-cysteinyl)-tyrosine (Tyr-Cys)"
FT /evidence="ECO:0000269|PubMed:19393666,
FT ECO:0000269|PubMed:22281743"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:3FO3"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:3FO3"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:3FO3"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:3FO3"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3FO3"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3FO3"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:4L3X"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:3FO3"
FT TURN 219..223
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3FO3"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:3FO3"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 271..277
FT /evidence="ECO:0007829|PDB:3FO3"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:3FO3"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:3FO3"
FT STRAND 307..317
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:3FO3"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:3FO3"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:3FO3"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:3FO3"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 360..369
FT /evidence="ECO:0007829|PDB:3FO3"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 391..395
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 407..411
FT /evidence="ECO:0007829|PDB:3FO3"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:3FO3"
FT TURN 435..438
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 448..486
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 490..512
FT /evidence="ECO:0007829|PDB:3FO3"
FT TURN 514..519
FT /evidence="ECO:0007829|PDB:3FO3"
FT HELIX 521..549
FT /evidence="ECO:0007829|PDB:3FO3"
SQ SEQUENCE 553 AA; 62345 MW; A9757797240FCCA7 CRC64;
MNDLNRLGRV GRWIAGAACL FLASAAHAEP GENLKPVDAM QCFDCHTQIE DMHTVGKHAT
VNCVHCHDAT EHVETASSRR MGERPVTRMD LEACATCHTA QFNSFVEVRH ESHPRLEKAT
PTSRSPMFDK LIAGHGFAFE HAEPRSHAFM LVDHFVVDRA YGGRFQFKNW QKVTDGMGAV
RGAWTVLTDA DPESSDQRRF LSQTATAANP VCLNCKTQDH ILDWAYMGDE HEAAKWSRTS
EVVEFARDLN HPLNCFMCHD PHSAGPRVVR DGLINAVVDR GLGTYPHDPV KSEQQGMTKV
TFQRGREDFR AIGLLDTADS NVMCAQCHVE YNCNPGYQLS DGSRVGMDDR RANHFFWANV
FDYKEAAQEI DFFDFRHATT GAALPKLQHP EAETFWGSVH ERNGVACADC HMPKVQLENG
KVYTSHSQRT PRDMMGQACL NCHAEWTEDQ ALYAIDYIKN YTHGKIVKSE YWLAKMIDLF
PVAKRAGVSE DVLNQARELH YDAHLYWEWW TAENSVGFHN PDQARESLMT SISKSKEAVS
LLNDAIDAQV ASR
