ID A0A5A7R3Q2_STRAF Unreviewed; 577 AA.
AC A0A5A7R3Q2;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peroxidase {ECO:0000256|ARBA:ARBA00012313};
DE EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313};
GN ORFNames=STAS_28232 {ECO:0000313|EMBL:GER50901.1};
OS Striga asiatica (Asiatic witchweed) (Buchnera asiatica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Orobanchaceae; Buchnereae; Striga.
OX NCBI_TaxID=4170 {ECO:0000313|EMBL:GER50901.1, ECO:0000313|Proteomes:UP000325081};
RN [1] {ECO:0000313|Proteomes:UP000325081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UVA1 {ECO:0000313|Proteomes:UP000325081};
RX PubMed=31522940; DOI=10.1016/j.cub.2019.07.086;
RA Yoshida S., Kim S., Wafula E.K., Tanskanen J., Kim Y.M., Honaas L.,
RA Yang Z., Spallek T., Conn C.E., Ichihashi Y., Cheong K., Cui S., Der J.P.,
RA Gundlach H., Jiao Y., Hori C., Ishida J.K., Kasahara H., Kiba T., Kim M.S.,
RA Koo N., Laohavisit A., Lee Y.H., Lumba S., McCourt P., Mortimer J.C.,
RA Mutuku J.M., Nomura T., Sasaki-Sekimoto Y., Seto Y., Wang Y., Wakatake T.,
RA Sakakibara H., Demura T., Yamaguchi S., Yoneyama K., Manabe R.I.,
RA Nelson D.C., Schulman A.H., Timko M.P., dePamphilis C.W., Choi D.,
RA Shirasu K.;
RT "Genome Sequence of Striga asiatica Provides Insight into the Evolution of
RT Plant Parasitism.";
RL Curr. Biol. 29:3041-3052.e4(2019).
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:0000256|ARBA:ARBA00000189};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR600823-
CC 3};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000256|PIRSR:PIRSR600823-3};
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000256|ARBA:ARBA00006873}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GER50901.1}.
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DR EMBL; BKCP01009404; GER50901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A7R3Q2; -.
DR Proteomes; UP000325081; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00693; secretory_peroxidase; 2.
DR Gene3D; 1.10.520.10; -; 2.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31388:SF3; PEROXIDASE 72; 1.
DR PANTHER; PTHR31388; PEROXIDASE 72-RELATED; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
DR PROSITE; PS00435; PEROXIDASE_1; 2.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR600823-3};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR600823-5}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR600823-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR600823-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:GER50901.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000325081};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..577
FT /note="peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023074313"
FT DOMAIN 27..327
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT DOMAIN 325..577
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT BINDING 199
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:0000256|PIRSR:PIRSR600823-3"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT SITE 64
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT DISULFID 37..117
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 70..75
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 123..323
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 206..231
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 577 AA; 62997 MW; 93E56A2AEB59C29F CRC64;
MASFPSYKAL LTCAVLLVLL SSSSAKLYGP DYYSIACPNL TDIVRNVVAR AIKNQARMGA
SLLRMHFHDC FINGCDGSIL LDDTPTLKGE KNAGPNKHSL RGYDVIDHIK EAVEKKCPGV
VSCADILAIA ARDSVNILGG PSWQVQLGRR DSRTANFSLA NSSLPSGLPS PQSNLTTLIM
NFKAHGLSVH DLVTLSGAHT IGQARCVSFR AHIYNDSNVD TTFANSLKSI CPSASGSNDN
NLAPLDAGSS TIFDNHYYVD LFYNKGLLHS DQELYNGNSS TAKHVVTYLH NTTAFAMDFA
KAMVKMGNMN PLTGSNGEIR KNCRRGCDAS VLLKDTSTFT GEQSATPNKN SIRKLEVIDQ
IKSEVETKCP GMVSCADILA IAARDAVDIL SGNKVCYMVE MGRLDSTTAN KTAANNLIPP
PTSSISDLIT NFKNHGLTET DLVLLAGAHT IGKARCTSFK NRLYNETNSL DKNFANNLRR
ICSPDDSKTG NNTADLDYQT PNVFDNHYYQ NIIANKTLLH SDHQLLNNSD TKYLVSKYSN
DNVGFSREFG QAMINMGRLK RTAGEKMEIR KTCWKQN
//
