ID A0A5A7QS49_STRAF Unreviewed; 1650 AA. AC A0A5A7QS49; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 24-JAN-2024, entry version 21. DE RecName: Full=peroxidase {ECO:0000256|ARBA:ARBA00012313}; DE EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313}; GN ORFNames=STAS_23809 {ECO:0000313|EMBL:GER46751.1}; 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:GER46751.1, 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. CC {ECO:0000256|RuleBase:RU004241}. 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:GER46751.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BKCP01007626; GER46751.1; -; Genomic_DNA. 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; IPR033905; Secretory_peroxidase. DR PANTHER; PTHR31388:SF3; PEROXIDASE 72; 1. DR PANTHER; PTHR31388; PEROXIDASE 72-RELATED; 1. DR Pfam; PF00141; peroxidase; 3. DR PRINTS; PR00458; PEROXIDASE. DR PRINTS; PR00461; PLPEROXIDASE. DR SUPFAM; SSF48113; Heme-dependent peroxidases; 3. DR PROSITE; PS00436; PEROXIDASE_2; 2. 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}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW 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:GER46751.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000325081}. FT DOMAIN 953..1216 FT /note="Plant heme peroxidase family profile" FT /evidence="ECO:0000259|PROSITE:PS50873" FT DOMAIN 1303..1616 FT /note="Plant heme peroxidase family profile" FT /evidence="ECO:0000259|PROSITE:PS50873" FT REGION 1..50 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 813..848 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1199..1221 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 9..47 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1350 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1" FT BINDING 1351 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 1354 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 1356 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 1358 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 1360 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 1372 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 1449 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2" FT BINDING 1479 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 1480 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 1511 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 1516 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT SITE 1346 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4" FT DISULFID 1313..1401 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 1352..1357 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 1407..1585 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 1486..1498 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" SQ SEQUENCE 1650 AA; 181199 MW; EC2011477A5E28AE CRC64; MMGFSPMGSG AGANSSSSTS NLSALAPPFT VDRSNPKLNS NPNLPYHDSP YTAEPYSHGW EYSIPSAPIV LESTGLASVP LPDDHRFSAA TTVSPTITHW STFSRVDKAS TSASYGDVKP YYSPYVPRLV GDESPLVEVD VTCYNKGPTS QIDYTRGVWD VDYEAGWAGN LGLNDGKRAN RVEIEGSFFE KSNIGDLQSY GHQLNQGWLD TEKNEKVSKE GSYGISNQIF NQVPDTGIHC GNSVVTQTKD NLCHEQNLGF FPYDSNKSLT SAYKSTYRES QELAVHKNSL DDQNSSTKCR KTVDKPFIGH VSSNMRSSAG VIRLPPANNG YIKQCTFARK STQCDSDESV RIANFGSISD SQLKEGSSET SLFGISNEGN FLTPLKELSI PLQSSDSLDR TCRAGFGSQS HDESIYGGFN MAGGNSVQTV KSNENSLDFV VDSPCWKGTS CSQFSTFDIE AGNSNNFKKK LDGYYESNHE AQQKNLDSVI DIDRTFFGKA SESNSNIGKN ESDTHCSSKD NSLLGDGKCR GWVAKENETL NEPNMPRKQS VLAKDLAGEF DAKTPDAKHL IDKVAKTISL NDVTEGGFVA VHAAEKVLAS PASQEDANER IKETDWKLHV PTVLKAMHNL SELLMFHLSG ESCSLEKENI ETLENTISNL NSCLHSKITE ASKKPKLNNP VRNSSGKLLE SRNMHTLEHE GNNSYFGKKD EKSPILSPLM DGIDMSSDDS MTKAIKKVLE ENFLLNEEIH SEALLFKNLW LDAEAKLCSI SYKARFDRMK IQMEQIRIKG SQDNEDCEGI SSDEVSISPA DITASEVGPK GPHDDQIVPK PALQDIPASS TGGPTDDVDA SVLARFNILK SREENAKPNK GFSGEQNEDP IVASLKLREE NFGKLMGMEE YENQPRSSEM NDACENTSLH EFHHSVTNND PTVHSCRNNL GRRDSSSSDW EHVLKDDFSC RTCVNVVSIV KEEVTSEYNN KDQFIASALL RLHFHDCFVR GCDGSILLDS TPGKLAEKDA PPNNPSLRKK AFALIDRIKG RLESLCPGVV SCADILAFAA RESVLLAGGP VYYLEGGRND GRISNATEAT QNLPKPQSNY KTLTEAFNGT ADPSLNKSSA DFLRGYCKRV PQPLVNMDDT PNAFDTKYYE YVLEGKVVLS SDNALLNNKD SRSRVKQYNE SSNKWFQDFA KAMEKMAKLS DTDPNNPDNE DCEGISSDEV SISPADITAS EVGPEGPHDD QIIPKPAMVP FVSINNEDCE GISSDEVSIS PADITASEVD PKGPHDDQIV PKPAFEDITS SRALQKDYYK NKCFGHGKQY NVEALVSDEV KSAYRSDKSI APALLRLHFH DCFVRGCDAS ILLDSTRGKP AEKVAPPNNP SIKQSTLDRI NYIKGQLESL CKGVVSCADI IAFAARDSVV LTGGKSYEVL GGRMDGRISN ASEAKSMVPS PQSNYKTLSD AFKKKNLTEV HMIALSGAHT IGQTNCSSVT KRPAPASCSR NPQKLVDMEN TPQKFDNGYY NRVLQRQALF SSDNALLNNK ISQTIVKRYN GSFDQWFHDF AIAMQKMGEI LDTDKSNHGE IRSDCRKFAE AMVKMGSIEV LTGSQGEVRA NCRVINGDCH EESSGKDILR MCAVDEDNLG MLPAARKGRR //