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Cytochrome c-552 (EC 1.7.2.2) (Cytochrome c nitrite reductase) (TvNiR)

 NIR_THIND               Reviewed;         553 AA.
L0DSL2; Q5F2I3;
29-APR-2015, integrated into UniProtKB/Swiss-Prot.
06-MAR-2013, sequence version 1.
18-JUL-2018, entry version 42.
RecName: Full=Cytochrome c-552;
EC=1.7.2.2 {ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:22281743};
AltName: Full=Cytochrome c nitrite reductase {ECO:0000303|PubMed:16500161, ECO:0000303|PubMed:19393666};
AltName: Full=TvNiR {ECO:0000303|PubMed:16500161};
Flags: Precursor;
Name=nir {ECO:0000312|EMBL:AGA31970.1};
OrderedLocusNames=TVNIR_0259 {ECO:0000312|EMBL:AGA31970.1};
Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 /
ALEN2).
Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
Ectothiorhodospiraceae; Thioalkalivibrio.
NCBI_TaxID=1255043 {ECO:0000312|EMBL:AGA31970.1};
[1] {ECO:0000312|EMBL:CAI56199.2}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-44,
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
SUBUNIT, AND ENZYME REGULATION.
STRAIN=DSM 14787 / UNIQEM 213 / ALEN2 {ECO:0000303|PubMed:16500161};
PubMed=16500161; DOI=10.1016/j.bbapap.2005.12.021;
Tikhonova T.V., Slutsky A., Antipov A.N., Boyko K.M., Polyakov K.M.,
Sorokin D.Y., Zvyagilskaya R.A., Popov V.O.;
"Molecular and catalytic properties of a novel cytochrome c nitrite
reductase from nitrate-reducing haloalkaliphilic sulfur-oxidizing
bacterium Thioalkalivibrio nitratireducens.";
Biochim. Biophys. Acta 1764:715-723(2006).
[2] {ECO:0000312|Proteomes:UP000010809}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 14787 / UNIQEM 213 / ALEN2
{ECO:0000312|Proteomes:UP000010809};
Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V.,
Sorokin D.Y., Ravin N.V., Popov V.O.;
"Complete sequence of Thioalkalivibrio nitratireducens.";
Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000244|PDB:2OT4, ECO:0000244|PDB:2ZO5, ECO:0000244|PDB:3D1I}
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 29-553 IN COMPLEXES WITH
CALCIUM; AZIDE; NITRITE AND HEME, COFACTOR, SUBUNIT, AND CROSS-LINK.
STRAIN=DSM 14787 / UNIQEM 213 / ALEN2 {ECO:0000303|PubMed:19393666};
PubMed=19393666; DOI=10.1016/j.jmb.2009.04.037;
Polyakov K.M., Boyko K.M., Tikhonova T.V., Slutsky A., Antipov A.N.,
Zvyagilskaya R.A., Popov A.N., Bourenkov G.P., Lamzin V.S.,
Popov V.O.;
"High-resolution structural analysis of a novel octaheme cytochrome c
nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio
nitratireducens.";
J. Mol. Biol. 389:846-862(2009).
[4] {ECO:0000244|PDB:3FO3, ECO:0000244|PDB:3MMO}
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 29-553 IN COMPLEXES WITH
CALCIUM; SULFITE; CYANIDE AND HEME, FUNCTION, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
STRAIN=DSM 14787 / UNIQEM 213 / ALEN2 {ECO:0000303|PubMed:20944237};
PubMed=20944237; DOI=10.1107/S0907444910031665;
Trofimov A.A., Polyakov K.M., Boyko K.M., Tikhonova T.V.,
Safonova T.N., Tikhonov A.V., Popov A.N., Popov V.O.;
"Structures of complexes of octahaem cytochrome c nitrite reductase
from Thioalkalivibrio nitratireducens with sulfite and cyanide.";
Acta Crystallogr. D 66:1043-1047(2010).
[5] {ECO:0000244|PDB:3LG1, ECO:0000244|PDB:3LGQ, ECO:0000244|PDB:3RKH}
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 33-551 IN COMPLEXES WITH
SULFITE; HYDROXYLAMINE; CALCIUM AND HEME, CATALYTIC ACTIVITY,
FUNCTION, COFACTOR, CROSS-LINK, AND SUBUNIT.
STRAIN=DSM 14787 / UNIQEM 213 / ALEN2 {ECO:0000303|PubMed:22281743};
PubMed=22281743; DOI=10.1107/S0907444911052632;
Trofimov A.A., Polyakov K.M., Tikhonova T.V., Tikhonov A.V.,
Safonova T.N., Boyko K.M., Dorovatovskii P.V., Popov V.O.;
"Covalent modifications of the catalytic tyrosine in octahaem
cytochrome c nitrite reductase and their effect on the enzyme
activity.";
Acta Crystallogr. D 68:144-153(2012).
-!- FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming
six electrons in the process (PubMed:16500161, PubMed:22281743).
Has very low activity toward hydroxylamine (PubMed:16500161). Has
even lower activity toward sulfite (PubMed:16500161,
PubMed:22281743). Sulfite reductase activity is maximal at neutral
pH (PubMed:20944237). {ECO:0000269|PubMed:16500161,
ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743}.
-!- CATALYTIC ACTIVITY: NH(3) + 2 H(2)O + 6 ferricytochrome c =
nitrite + 6 ferrocytochrome c + 7 H(+).
{ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:22281743}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:16500161,
ECO:0000269|PubMed:19393666, ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743};
Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000269|PubMed:16500161,
ECO:0000269|PubMed:19393666, ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743};
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:16500161,
ECO:0000269|PubMed:19393666, ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743};
Note=Binds 8 heme groups covalently per monomer.
{ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237, ECO:0000269|PubMed:22281743};
-!- ENZYME REGULATION: Inhibited by azide and cyanide. Subject to
competitive inhibition by sulfite. {ECO:0000269|PubMed:16500161}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=16700 uM for nitrite {ECO:0000269|PubMed:16500161};
KM=16400 uM for hydroxylamine {ECO:0000269|PubMed:16500161};
Vmax=4080 umol/min/mg enzyme toward nitrite
{ECO:0000269|PubMed:16500161};
Vmax=45 umol/min/mg enzyme toward hydroxylamine
{ECO:0000269|PubMed:16500161};
pH dependence:
Optimum pH is 7-10 for nitrite reduction, and the optimum pH is
7 for sulfite reduction with only 20% residual activity at pH
7.8. {ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:20944237};
Temperature dependence:
Optimum temperature is 80 degrees Celsius.
{ECO:0000269|PubMed:16500161};
-!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
-!- SUBUNIT: Homohexamer. Dimer of trimers.
{ECO:0000269|PubMed:16500161, ECO:0000269|PubMed:19393666,
ECO:0000305|PubMed:20944237, ECO:0000305|PubMed:22281743}.
-!- SUBCELLULAR LOCATION: Periplasm.
-!- PTM: The thioether cross-link between Tyr-331 and Cys-333 may play
a structural role in the active site cavity (PubMed:19393666).
Besides, it may lower the pKa of the Tyr hydroxyl group
(PubMed:19393666). An additional covalent bond between Tyr-331 and
Gln-388 has been observed in some protein crystals, but this may
be an artifact that is due to the formation of tyrosyl radicals
when the protein is exposed to oxygen (PubMed:22281743).
{ECO:0000269|PubMed:19393666, ECO:0000269|PubMed:22281743}.
-!- SIMILARITY: Belongs to the cytochrome c-552 family. {ECO:0000305}.
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EMBL; AJ880678; CAI56199.2; -; Genomic_DNA.
EMBL; CP003989; AGA31970.1; -; Genomic_DNA.
RefSeq; WP_015257125.1; NC_019902.2.
PDB; 2OT4; X-ray; 1.50 A; A/B=29-553.
PDB; 2ZO5; X-ray; 1.70 A; A/B=29-553.
PDB; 3D1I; X-ray; 1.80 A; A/B=29-553.
PDB; 3F29; X-ray; 2.00 A; A/B=29-553.
PDB; 3FO3; X-ray; 1.40 A; A/B=29-553.
PDB; 3GM6; X-ray; 1.80 A; A/B=29-553.
PDB; 3LG1; X-ray; 1.95 A; A/B=29-553.
PDB; 3LGQ; X-ray; 1.80 A; A/B=29-553.
PDB; 3MMO; X-ray; 1.55 A; A/B=29-553.
PDB; 3OWM; X-ray; 1.65 A; A/B=33-551.
PDB; 3RKH; X-ray; 1.83 A; A/B=33-551.
PDB; 3S7W; X-ray; 1.79 A; A/B=33-551.
PDB; 3SCE; X-ray; 1.45 A; A/B=33-551.
PDB; 3UU9; X-ray; 2.20 A; A/B=33-552.
PDB; 4L38; X-ray; 1.80 A; A/B=33-551.
PDB; 4L3X; X-ray; 1.85 A; A/B=33-551.
PDB; 4L3Y; X-ray; 1.95 A; A/B=33-551.
PDB; 4L3Z; X-ray; 1.85 A; A/B=33-551.
PDB; 4Q0T; X-ray; 1.70 A; A/B=30-553.
PDB; 4Q17; X-ray; 1.75 A; A/B=29-553.
PDB; 4Q1O; X-ray; 1.75 A; A/B=29-553.
PDB; 4Q4U; X-ray; 1.62 A; A/B=33-553.
PDB; 4Q5B; X-ray; 1.80 A; A/B=33-553.
PDB; 4Q5C; X-ray; 1.62 A; A/B=33-553.
PDBsum; 2OT4; -.
PDBsum; 2ZO5; -.
PDBsum; 3D1I; -.
PDBsum; 3F29; -.
PDBsum; 3FO3; -.
PDBsum; 3GM6; -.
PDBsum; 3LG1; -.
PDBsum; 3LGQ; -.
PDBsum; 3MMO; -.
PDBsum; 3OWM; -.
PDBsum; 3RKH; -.
PDBsum; 3S7W; -.
PDBsum; 3SCE; -.
PDBsum; 3UU9; -.
PDBsum; 4L38; -.
PDBsum; 4L3X; -.
PDBsum; 4L3Y; -.
PDBsum; 4L3Z; -.
PDBsum; 4Q0T; -.
PDBsum; 4Q17; -.
PDBsum; 4Q1O; -.
PDBsum; 4Q4U; -.
PDBsum; 4Q5B; -.
PDBsum; 4Q5C; -.
ProteinModelPortal; L0DSL2; -.
SMR; L0DSL2; -.
DrugBank; DB02580; 1-(2-Methoxy-Ethoxy)-2-{2-[2-(2-Methoxy-Ethoxy]-Ethoxy}-Ethane.
EnsemblBacteria; AGA31970; AGA31970; TVNIR_0259.
KEGG; tni:TVNIR_0259; -.
PATRIC; fig|1255043.3.peg.260; -.
OrthoDB; POG091H0H2F; -.
BioCyc; TNIT1255043:G1HDO-251-MONOMER; -.
UniPathway; UPA00653; -.
Proteomes; UP000010809; Chromosome.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0042279; F:nitrite reductase (cytochrome, ammonia-forming) activity; IDA:UniProtKB.
GO; GO:0097164; P:ammonium ion metabolic process; IDA:UniProtKB.
GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
InterPro; IPR003321; Cyt_c552.
InterPro; IPR011031; Multihaem_cyt.
InterPro; IPR036280; Multihaem_cyt_sf.
PANTHER; PTHR30633; PTHR30633; 1.
Pfam; PF02335; Cytochrom_C552; 1.
PIRSF; PIRSF000243; Cyt_c552; 1.
SUPFAM; SSF48695; SSF48695; 3.
PROSITE; PS51008; MULTIHEME_CYTC; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Direct protein sequencing;
Electron transport; Heme; Iron; Metal-binding; Oxidoreductase;
Periplasm; Reference proteome; Signal; Thioether bond; Transport.
SIGNAL 1 28 {ECO:0000269|PubMed:16500161}.
CHAIN 29 553 Cytochrome c-552.
/FTId=PRO_5001089214.
METAL 46 46 Iron (heme 1 axial ligand); via tele
nitrogen. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 58 58 Iron (heme 3 axial ligand); via tele
nitrogen. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 67 67 Iron (heme 2 axial ligand); via tele
nitrogen. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 72 72 Iron (heme 1 axial ligand); via tele
nitrogen. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 98 98 Iron (heme 3 axial ligand); via tele
nitrogen. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 147 147 Iron (heme 5 axial ligand); via tele
nitrogen. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 216 216 Iron (heme 6 axial ligand).
{ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 259 259 Iron (heme 4 axial ligand); via tele
nitrogen. {ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 262 262 Iron (heme 2 axial ligand); via tele
nitrogen. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 328 328 Iron (heme 5 axial ligand); via tele
nitrogen. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 330 330 Calcium. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 331 331 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 386 386 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 388 388 Calcium. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 400 400 Iron (heme 7 axial ligand); via tele
nitrogen. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 411 411 Iron (heme 8 axial ligand); via tele
nitrogen. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 426 426 Iron (heme 4 axial ligand); via tele
nitrogen. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 443 443 Iron (heme 7 axial ligand); via tele
nitrogen. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
METAL 519 519 Iron (heme 8 axial ligand); via tele
nitrogen. {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 42 42 Heme 1 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 45 45 Heme 1 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 63 63 Heme 2 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 66 66 Heme 2 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 94 94 Heme 3 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 97 97 Heme 3 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 212 212 Heme 6 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 215 215 Heme 6 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 255 255 Heme 4 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 258 258 Heme 4 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 324 324 Heme 5 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 327 327 Heme 5 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 407 407 Heme 8 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 410 410 Heme 8 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 439 439 Heme 7 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
BINDING 442 442 Heme 7 (covalent). {ECO:0000244|PDB:4L38,
ECO:0000244|PDB:4L3X,
ECO:0000244|PDB:4L3Y,
ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:20944237,
ECO:0000269|PubMed:22281743}.
CROSSLNK 331 333 3'-(S-cysteinyl)-tyrosine (Tyr-Cys).
{ECO:0000269|PubMed:19393666,
ECO:0000269|PubMed:22281743}.
HELIX 39 43 {ECO:0000244|PDB:3FO3}.
HELIX 47 55 {ECO:0000244|PDB:3FO3}.
TURN 57 60 {ECO:0000244|PDB:3FO3}.
HELIX 63 65 {ECO:0000244|PDB:3FO3}.
HELIX 70 75 {ECO:0000244|PDB:3FO3}.
HELIX 92 95 {ECO:0000244|PDB:3FO3}.
HELIX 99 106 {ECO:0000244|PDB:3FO3}.
STRAND 117 120 {ECO:0000244|PDB:3FO3}.
HELIX 128 132 {ECO:0000244|PDB:3FO3}.
HELIX 136 139 {ECO:0000244|PDB:3FO3}.
HELIX 147 149 {ECO:0000244|PDB:3FO3}.
HELIX 150 156 {ECO:0000244|PDB:3FO3}.
TURN 158 160 {ECO:0000244|PDB:3FO3}.
STRAND 165 169 {ECO:0000244|PDB:3FO3}.
HELIX 170 174 {ECO:0000244|PDB:3FO3}.
HELIX 176 181 {ECO:0000244|PDB:3FO3}.
HELIX 183 185 {ECO:0000244|PDB:3FO3}.
STRAND 187 190 {ECO:0000244|PDB:3FO3}.
STRAND 200 203 {ECO:0000244|PDB:4L3X}.
HELIX 210 215 {ECO:0000244|PDB:3FO3}.
TURN 219 223 {ECO:0000244|PDB:3FO3}.
HELIX 226 228 {ECO:0000244|PDB:3FO3}.
HELIX 242 247 {ECO:0000244|PDB:3FO3}.
HELIX 255 257 {ECO:0000244|PDB:3FO3}.
TURN 261 263 {ECO:0000244|PDB:3FO3}.
STRAND 266 268 {ECO:0000244|PDB:3FO3}.
HELIX 271 277 {ECO:0000244|PDB:3FO3}.
TURN 278 280 {ECO:0000244|PDB:3FO3}.
HELIX 289 294 {ECO:0000244|PDB:3FO3}.
STRAND 297 304 {ECO:0000244|PDB:3FO3}.
STRAND 307 317 {ECO:0000244|PDB:3FO3}.
HELIX 320 324 {ECO:0000244|PDB:3FO3}.
TURN 325 327 {ECO:0000244|PDB:3FO3}.
STRAND 331 334 {ECO:0000244|PDB:3FO3}.
TURN 339 341 {ECO:0000244|PDB:3FO3}.
HELIX 350 352 {ECO:0000244|PDB:3FO3}.
STRAND 353 355 {ECO:0000244|PDB:3FO3}.
HELIX 360 369 {ECO:0000244|PDB:3FO3}.
TURN 378 380 {ECO:0000244|PDB:3FO3}.
HELIX 391 395 {ECO:0000244|PDB:3FO3}.
HELIX 399 402 {ECO:0000244|PDB:3FO3}.
HELIX 407 411 {ECO:0000244|PDB:3FO3}.
STRAND 418 420 {ECO:0000244|PDB:3FO3}.
HELIX 431 433 {ECO:0000244|PDB:3FO3}.
TURN 435 438 {ECO:0000244|PDB:3FO3}.
HELIX 439 442 {ECO:0000244|PDB:3FO3}.
HELIX 448 486 {ECO:0000244|PDB:3FO3}.
HELIX 490 512 {ECO:0000244|PDB:3FO3}.
TURN 514 519 {ECO:0000244|PDB:3FO3}.
HELIX 521 549 {ECO:0000244|PDB:3FO3}.
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


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