PERL_BOVIN
ID PERL_BOVIN Reviewed; 712 AA.
AC P80025;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Lactoperoxidase {ECO:0000303|PubMed:19339248};
DE Short=LPO {ECO:0000303|PubMed:19339248};
DE EC=1.11.1.7 {ECO:0000269|PubMed:354515, ECO:0000269|PubMed:5338806, ECO:0000305|PubMed:19167310, ECO:0000305|PubMed:19339248, ECO:0000305|PubMed:33882424};
DE Flags: Precursor;
GN Name=LPO;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2222811; DOI=10.1089/dna.1990.9.499;
RA Dull T.J., Uyeda C., Strosberg A.D., Nedwin G., Seilhamer J.J.;
RT "Molecular cloning of cDNAs encoding bovine and human lactoperoxidase.";
RL DNA Cell Biol. 9:499-509(1990).
RN [2]
RP PROTEIN SEQUENCE OF 101-712, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Milk;
RX PubMed=2050150; DOI=10.1111/j.1432-1033.1991.tb16073.x;
RA Cals M.-M., Mailliart P., Brignon G., Anglade P., Ribadeau-Dumas B.;
RT "Primary structure of bovine lactoperoxidase, a fourth member of a
RT mammalian heme peroxidase family.";
RL Eur. J. Biochem. 198:733-739(1991).
RN [3]
RP CIRCULAR DICHROISM ANALYSIS, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=10924350; DOI=10.1006/bbrc.2000.3217;
RA Watanabe S., Murata S., Kumura H., Nakamura S., Bollen A., Moguilevsky N.,
RA Shimazaki K.;
RT "Bovine lactoperoxidase and its recombinant: comparison of structure and
RT some biochemical properties.";
RL Biochem. Biophys. Res. Commun. 274:756-761(2000).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=5338806; DOI=10.1042/bj1000382;
RA Oram J.D., Reiter B.;
RT "The inhibition of streptococci by lactoperoxidase, thiocyanate and
RT hydrogen peroxide. The oxidation of thiocyanate and the nature of the
RT inhibitory compound.";
RL Biochem. J. 100:382-388(1966).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=354515; DOI=10.1128/aac.13.6.1006;
RA Thomas E.L., Aune T.M.;
RT "Oxidation of Escherichia coli sulfhydryl components by the peroxidase-
RT hydrogen peroxide-iodide antimicrobial system.";
RL Antimicrob. Agents Chemother. 13:1006-1010(1978).
RN [6]
RP COVALENT HEME ATTACHMENT.
RX PubMed=9083001; DOI=10.1074/jbc.272.14.8857;
RA DePillis G.D., Ozaki S., Kuo J.M., Maltby D.A., Ortiz de Montellano P.R.;
RT "Autocatalytic processing of heme by lactoperoxidase produces the native
RT protein-bound prosthetic group.";
RL J. Biol. Chem. 272:8857-8860(1997).
RN [7]
RP COVALENT HEME ATTACHMENT.
RC TISSUE=Milk;
RX PubMed=9774411; DOI=10.1074/jbc.273.43.27968;
RA Rae T.D., Goff H.M.;
RT "The heme prosthetic group of lactoperoxidase. Structural characteristics
RT of heme l and heme l-peptides.";
RL J. Biol. Chem. 273:27968-27977(1998).
RN [8]
RP COVALENT HEME ATTACHMENT, AND MUTAGENESIS OF ASP-225 AND GLU-375.
RX PubMed=11597409; DOI=10.1016/s0960-894x(01)00533-9;
RA Suriano G., Watanabe S., Ghibaudi E.M., Bollen A., Ferrari R.P.,
RA Moguilevsky N.;
RT "Glu375Gln and Asp225Val mutants: about the nature of the covalent linkages
RT between heme group and apo-protein in bovine lactoperoxidase.";
RL Bioorg. Med. Chem. Lett. 11:2827-2831(2001).
RN [9]
RP COVALENT HEME ATTACHMENT, AND MUTAGENESIS OF ASP-225 AND GLU-375.
RX PubMed=11756449; DOI=10.1074/jbc.m109523200;
RA Colas C., Kuo J.M., Ortiz de Montellano P.R.;
RT "Asp-225 and Glu-375 in autocatalytic attachment of the prosthetic heme
RT group of lactoperoxidase.";
RL J. Biol. Chem. 277:7191-7200(2002).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 130-712 IN COMPLEX WITH
RP HYPOTHIOCYANATE, GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 AND ASN-449,
RP PHOSPHORYLATION AT SER-315, COFACTOR, CALCIUM-BINDING SITES, DISULFIDE
RP BONDS, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19167310; DOI=10.1016/j.bpj.2008.09.019;
RA Singh A.K., Singh N., Sharma S., Shin K., Takase M., Kaur P.,
RA Srinivasan A., Singh T.P.;
RT "Inhibition of lactoperoxidase by its own catalytic product: crystal
RT structure of the hypothiocyanate-inhibited bovine lactoperoxidase at 2.3-A
RT resolution.";
RL Biophys. J. 96:646-654(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 118-712 IN COMPLEX WITH
RP THIOCYANATE; CALCIUM AND HEME, COFACTOR, CALCIUM-BINDING SITES,
RP PHOSPHORYLATION AT SER-315, GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 AND
RP ASN-449, DISULFIDE BONDS, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19339248; DOI=10.1074/jbc.m807644200;
RA Sheikh I.A., Singh A.K., Singh N., Sinha M., Singh S.B., Bhushan A.,
RA Kaur P., Srinivasan A., Sharma S., Singh T.P.;
RT "Structural evidence of substrate specificity in mammalian peroxidases:
RT structure of the thiocyanate complex with lactoperoxidase and its
RT interactions at 2.4 A resolution.";
RL J. Biol. Chem. 284:14849-14856(2009).
RN [12] {ECO:0007744|PDB:7DLQ, ECO:0007744|PDB:7DN6, ECO:0007744|PDB:7DN7}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 118-712 IN COMPLEX WITH HYDROGEN
RP PEROXIDE; IODIDE; CALCIUM AND HEME, COFACTOR, DISULFIDE BONDS, FUNCTION,
RP AND CATALYTIC ACTIVITY.
RX PubMed=33882424; DOI=10.1016/j.jinorgbio.2021.111461;
RA Singh P.K., Sharma P., Bhushan A., Kaur P., Sharma S., Singh T.P.;
RT "Structure of a ternary complex of lactoperoxidase with iodide and hydrogen
RT peroxide at 1.77A resolution.";
RL J. Inorg. Biochem. 220:111461-111461(2021).
CC -!- FUNCTION: Heme-containing oxidoreductase which catalyzes the conversion
CC of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid
CC (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (PubMed:5338806)
CC (Probable). Also involved in the conversion of iodide (I(-)) into
CC hypoiodite (IO(-)) in the presence of H2O2 (PubMed:354515) (Probable).
CC Responsible for the inactivation of a wide range of micro-organisms and
CC hence, important component of defense mechanism (PubMed:5338806,
CC PubMed:354515). The lactoperoxidase-SCN(-)-H2O2 system shows
CC antibacterial properties against some streptococci strains
CC (PubMed:5338806). The lactoperoxidase-I(-)-H2O2 system shows
CC antibacterial properties against E.coli (PubMed:354515). May protect
CC the udder from infection and may promote growth in newborns (By
CC similarity). May be implicated in airway host defense against infection
CC (By similarity). May contribute to maintaining an appropriate H2O2
CC cellular level, therefore protecting cells from H2O2-caused injuries
CC and inflammation (By similarity). {ECO:0000250|UniProtKB:A0A452E9Y6,
CC ECO:0000250|UniProtKB:P22079, ECO:0000250|UniProtKB:Q5SW46,
CC ECO:0000269|PubMed:354515, ECO:0000269|PubMed:5338806,
CC ECO:0000305|PubMed:19167310, ECO:0000305|PubMed:19339248,
CC ECO:0000305|PubMed:33882424}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC Evidence={ECO:0000269|PubMed:354515, ECO:0000269|PubMed:5338806,
CC ECO:0000305|PubMed:19167310, ECO:0000305|PubMed:19339248,
CC ECO:0000305|PubMed:33882424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56137;
CC Evidence={ECO:0000305|PubMed:19167310, ECO:0000305|PubMed:19339248,
CC ECO:0000305|PubMed:33882424, ECO:0000305|PubMed:354515,
CC ECO:0000305|PubMed:5338806};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O2 + thiocyanate = H2O + hypothiocyanous acid;
CC Xref=Rhea:RHEA:69416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:18022, ChEBI:CHEBI:133907;
CC Evidence={ECO:0000269|PubMed:5338806, ECO:0000305|PubMed:19167310,
CC ECO:0000305|PubMed:19339248};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69417;
CC Evidence={ECO:0000305|PubMed:19167310, ECO:0000305|PubMed:19339248,
CC ECO:0000305|PubMed:5338806};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + iodide = H2O + hypoiodite; Xref=Rhea:RHEA:69420,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382,
CC ChEBI:CHEBI:29232; Evidence={ECO:0000269|PubMed:354515,
CC ECO:0000305|PubMed:33882424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69421;
CC Evidence={ECO:0000305|PubMed:33882424, ECO:0000305|PubMed:354515};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248,
CC ECO:0000269|PubMed:33882424};
CC Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000269|PubMed:19167310,
CC ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248,
CC ECO:0000269|PubMed:33882424};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per
CC heterodimer. {ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248,
CC ECO:0000269|PubMed:33882424};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2050150}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q5SW46}.
CC -!- TISSUE SPECIFICITY: Mammary gland; milk. {ECO:0000269|PubMed:2050150}.
CC -!- MISCELLANEOUS: Thiocyanate (SCN(-)) and hypothiocyanite (OSCN(-)) are
CC bound in the distal heme cavity (PubMed:19167310, PubMed:19339248). The
CC iodide ion (I(-)) occupies a position which is stabilized by the
CC interactions with heme moiety, His-226, Arg-372 and Glu-375
CC (PubMed:33882424). Hydrogen peroxide is held between the heme iron and
CC His-226 (PubMed:33882424). {ECO:0000269|PubMed:19167310,
CC ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424}.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/LPO/";
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DR EMBL; M58150; AAA62714.1; -; mRNA.
DR PIR; A35828; A35828.
DR RefSeq; NP_776358.1; NM_173933.2.
DR RefSeq; XP_010814001.1; XM_010815699.2.
DR RefSeq; XP_010814003.1; XM_010815701.2.
DR RefSeq; XP_015313999.1; XM_015458513.1.
DR PDB; 2IPS; X-ray; 3.10 A; A=118-712.
DR PDB; 2NQX; X-ray; 2.95 A; A=118-712.
DR PDB; 2PT3; X-ray; 2.34 A; A=118-712.
DR PDB; 2PUM; X-ray; 2.70 A; A=118-712.
DR PDB; 2QPK; X-ray; 2.34 A; A=118-712.
DR PDB; 2QQT; X-ray; 2.50 A; A=118-712.
DR PDB; 2QRB; X-ray; 2.50 A; A=118-712.
DR PDB; 3BXI; X-ray; 2.30 A; A=118-712.
DR PDB; 3ERI; X-ray; 2.50 A; A=118-712.
DR PDB; 3GC1; X-ray; 2.50 A; A=118-712.
DR PDB; 3GCJ; X-ray; 2.34 A; A=118-712.
DR PDB; 3GCK; X-ray; 2.90 A; A=118-712.
DR PDB; 3GCL; X-ray; 2.50 A; A=118-712.
DR PDB; 3I6N; X-ray; 2.70 A; A=118-712.
DR PDB; 3KRQ; X-ray; 2.25 A; A=118-712.
DR PDB; 3NYH; X-ray; 1.77 A; A=118-712.
DR PDB; 3PY4; X-ray; 2.42 A; A=118-712.
DR PDB; 3R4X; X-ray; 2.01 A; A=118-712.
DR PDB; 3R5O; X-ray; 2.60 A; A=118-712.
DR PDB; 3S4F; X-ray; 2.00 A; A=118-712.
DR PDB; 3TGY; X-ray; 2.35 A; A=118-712.
DR PDB; 3UBA; X-ray; 2.65 A; A=118-712.
DR PDB; 3V6Q; X-ray; 2.00 A; A=118-712.
DR PDB; 4GM7; X-ray; 2.60 A; A=118-712.
DR PDB; 4KSZ; X-ray; 1.98 A; A=118-712.
DR PDB; 4NJB; X-ray; 2.31 A; A=118-712.
DR PDB; 4PNX; X-ray; 2.41 A; A=118-712.
DR PDB; 5B72; X-ray; 1.98 A; A=118-712.
DR PDB; 5GH0; X-ray; 2.30 A; A=118-712.
DR PDB; 5GLS; X-ray; 1.93 A; A=118-712.
DR PDB; 5WV3; X-ray; 2.07 A; A=118-712.
DR PDB; 5ZGS; X-ray; 2.20 A; A=118-712.
DR PDB; 6A4Y; X-ray; 1.92 A; A=118-712.
DR PDB; 6KMK; X-ray; 2.30 A; A=118-712.
DR PDB; 6KY7; X-ray; 2.27 A; A=118-712.
DR PDB; 6L2J; X-ray; 1.93 A; A=118-712.
DR PDB; 6L5G; X-ray; 2.50 A; A=118-712.
DR PDB; 6L9T; X-ray; 1.89 A; A=118-712.
DR PDB; 6LCO; X-ray; 2.00 A; A=118-712.
DR PDB; 6M7E; X-ray; 2.42 A; A=118-712.
DR PDB; 7C75; X-ray; 2.70 A; A=118-712.
DR PDB; 7D52; X-ray; 2.20 A; A=118-712.
DR PDB; 7DLQ; X-ray; 1.77 A; A=118-712.
DR PDB; 7DMR; X-ray; 2.20 A; A=118-712.
DR PDB; 7DN6; X-ray; 1.70 A; A=118-712.
DR PDB; 7DN7; X-ray; 1.70 A; A=118-712.
DR PDB; 7VIN; X-ray; 1.89 A; A=118-712.
DR PDBsum; 2IPS; -.
DR PDBsum; 2NQX; -.
DR PDBsum; 2PT3; -.
DR PDBsum; 2PUM; -.
DR PDBsum; 2QPK; -.
DR PDBsum; 2QQT; -.
DR PDBsum; 2QRB; -.
DR PDBsum; 3BXI; -.
DR PDBsum; 3ERI; -.
DR PDBsum; 3GC1; -.
DR PDBsum; 3GCJ; -.
DR PDBsum; 3GCK; -.
DR PDBsum; 3GCL; -.
DR PDBsum; 3I6N; -.
DR PDBsum; 3KRQ; -.
DR PDBsum; 3NYH; -.
DR PDBsum; 3PY4; -.
DR PDBsum; 3R4X; -.
DR PDBsum; 3R5O; -.
DR PDBsum; 3S4F; -.
DR PDBsum; 3TGY; -.
DR PDBsum; 3UBA; -.
DR PDBsum; 3V6Q; -.
DR PDBsum; 4GM7; -.
DR PDBsum; 4KSZ; -.
DR PDBsum; 4NJB; -.
DR PDBsum; 4PNX; -.
DR PDBsum; 5B72; -.
DR PDBsum; 5GH0; -.
DR PDBsum; 5GLS; -.
DR PDBsum; 5WV3; -.
DR PDBsum; 5ZGS; -.
DR PDBsum; 6A4Y; -.
DR PDBsum; 6KMK; -.
DR PDBsum; 6KY7; -.
DR PDBsum; 6L2J; -.
DR PDBsum; 6L5G; -.
DR PDBsum; 6L9T; -.
DR PDBsum; 6LCO; -.
DR PDBsum; 6M7E; -.
DR PDBsum; 7C75; -.
DR PDBsum; 7D52; -.
DR PDBsum; 7DLQ; -.
DR PDBsum; 7DMR; -.
DR PDBsum; 7DN6; -.
DR PDBsum; 7DN7; -.
DR PDBsum; 7VIN; -.
DR AlphaFoldDB; P80025; -.
DR SMR; P80025; -.
DR STRING; 9913.ENSBTAP00000016986; -.
DR BindingDB; P80025; -.
DR ChEMBL; CHEMBL2295561; -.
DR DrugCentral; P80025; -.
DR PeroxiBase; 3331; BtLPO.
DR iPTMnet; P80025; -.
DR PaxDb; P80025; -.
DR PeptideAtlas; P80025; -.
DR PRIDE; P80025; -.
DR Ensembl; ENSBTAT00000016986; ENSBTAP00000016986; ENSBTAG00000012780.
DR GeneID; 280844; -.
DR KEGG; bta:280844; -.
DR CTD; 4025; -.
DR VEuPathDB; HostDB:ENSBTAG00000012780; -.
DR VGNC; VGNC:30970; LPO.
DR eggNOG; KOG2408; Eukaryota.
DR GeneTree; ENSGT00940000160488; -.
DR InParanoid; P80025; -.
DR OMA; QNKMMTR; -.
DR OrthoDB; 276568at2759; -.
DR TreeFam; TF314316; -.
DR BRENDA; 1.11.1.7; 908.
DR Reactome; R-BTA-8941413; Events associated with phagocytolytic activity of PMN cells.
DR SABIO-RK; P80025; -.
DR EvolutionaryTrace; P80025; -.
DR PRO; PR:P80025; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000012780; Expressed in saliva-secreting gland and 40 other tissues.
DR ExpressionAtlas; P80025; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0036393; F:thiocyanate peroxidase activity; IDA:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 1.10.640.10; -; 1.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR029587; LPO.
DR PANTHER; PTHR11475:SF67; PTHR11475:SF67; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Calcium;
KW Cleavage on pair of basic residues; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Nitration; Oxidoreductase; Peroxidase; Phosphoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..100
FT /evidence="ECO:0000269|PubMed:2050150"
FT /id="PRO_0000023647"
FT CHAIN 101..712
FT /note="Lactoperoxidase"
FT /id="PRO_0000023648"
FT ACT_SITE 226
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 225
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248,
FT ECO:0000269|PubMed:33882424"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248,
FT ECO:0000269|PubMed:33882424"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248,
FT ECO:0000269|PubMed:33882424"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248,
FT ECO:0000269|PubMed:33882424"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:19167310, ECO:0000269|PubMed:19339248,
FT ECO:0000269|PubMed:33882424"
FT BINDING 375
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424"
FT BINDING 468
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424"
FT SITE 372
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248"
FT MOD_RES 482
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11678"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248"
FT DISULFID 123..284
FT /evidence="ECO:0000269|PubMed:33882424"
FT DISULFID 132..145
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424"
FT DISULFID 246..256
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424"
FT DISULFID 250..274
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424"
FT DISULFID 354..365
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424"
FT DISULFID 573..630
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424"
FT DISULFID 671..696
FT /evidence="ECO:0000269|PubMed:19167310,
FT ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:33882424"
FT MUTAGEN 225
FT /note="D->E: Partially bound heme and decrease in activity.
FT Loss of heme binding and activity; when associated with D-
FT 375."
FT /evidence="ECO:0000269|PubMed:11597409,
FT ECO:0000269|PubMed:11756449"
FT MUTAGEN 225
FT /note="D->V: Partially bound heme."
FT /evidence="ECO:0000269|PubMed:11597409,
FT ECO:0000269|PubMed:11756449"
FT MUTAGEN 375
FT /note="E->D: Partially bound heme. Loss of heme binding and
FT activity; when associated with E-225."
FT /evidence="ECO:0000269|PubMed:11597409,
FT ECO:0000269|PubMed:11756449"
FT MUTAGEN 375
FT /note="E->Q: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:11597409,
FT ECO:0000269|PubMed:11756449"
FT CONFLICT 449
FT /note="N -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3R4X"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:5B72"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:7DN6"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:3NYH"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:3S4F"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:3GC1"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:7DN6"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:5GLS"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:2PT3"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:4PNX"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:7DN6"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:7DN6"
FT TURN 371..374
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 377..400
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 406..427
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 429..434
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:3GC1"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 464..470
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:3NYH"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 501..504
FT /evidence="ECO:0007829|PDB:7DN6"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 510..518
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:7DLQ"
FT HELIX 532..535
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:6LCO"
FT TURN 541..543
FT /evidence="ECO:0007829|PDB:7DLQ"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 550..560
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 566..572
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 581..588
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 591..601
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 609..615
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 626..641
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:3GC1"
FT TURN 650..652
FT /evidence="ECO:0007829|PDB:3S4F"
FT HELIX 655..661
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 666..673
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 678..682
FT /evidence="ECO:0007829|PDB:7DN6"
FT TURN 689..692
FT /evidence="ECO:0007829|PDB:7DN6"
FT STRAND 693..695
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:7DN6"
FT HELIX 705..707
FT /evidence="ECO:0007829|PDB:7DN6"
SQ SEQUENCE 712 AA; 80642 MW; 28EED4C0C8420E6D CRC64;
MWVCLQLPVF LASVTLFEVA ASDTIAQAAS TTTISDAVSK VKIQVNKAFL DSRTRLKTTL
SSEAPTTQQL SEYFKHAKGR TRTAIRNGQV WEESLKRLRR DTTLTNVTDP SLDLTALSWE
VGCGAPVPLV KCDENSPYRT ITGDCNNRRS PALGAANRAL ARWLPAEYED GLALPFGWTQ
RKTRNGFRVP LAREVSNKIV GYLDEEGVLD QNRSLLFMQW GQIVDHDLDF APETELGSNE
HSKTQCEEYC IQGDNCFPIM FPKNDPKLKT QGKCMPFFRA GFVCPTPPYQ SLAREQINAV
TSFLDASLVY GSEPSLASRL RNLSSPLGLM AVNQEAWDHG LAYLPFNNKK PSPCEFINTT
ARVPCFLAGD FRASEQILLA TAHTLLLREH NRLARELKKL NPHWNGEKLY QEARKILGAF
IQIITFRDYL PIVLGSEMQK WIPPYQGYNN SVDPRISNVF TFAFRFGHME VPSTVSRLDE
NYQPWGPEAE LPLHTLFFNT WRIIKDGGID PLVRGLLAKK SKLMNQDKMV TSELRNKLFQ
PTHKIHGFDL AAINLQRCRD HGMPGYNSWR GFCGLSQPKT LKGLQTVLKN KILAKKLMDL
YKTPDNIDIW IGGNAEPMVE RGRVGPLLAC LLGRQFQQIR DGDRFWWENP GVFTEKQRDS
LQKVSFSRLI CDNTHITKVP LHAFQANNYP HDFVDCSTVD KLDLSPWASR EN
