ID A0A960TU14_UNCXX Unreviewed; 321 AA. AC A0A960TU14; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 29-MAY-2024, entry version 5. DE SubName: Full=Catalase-peroxidase {ECO:0000313|EMBL:MCB1151607.1}; DE Flags: Fragment; GN ORFNames=KDK88_08650 {ECO:0000313|EMBL:MCB1151607.1}; OS bacterium. OC Bacteria. OX NCBI_TaxID=1869227 {ECO:0000313|EMBL:MCB1151607.1, ECO:0000313|Proteomes:UP000712979}; RN [1] {ECO:0000313|EMBL:MCB1151607.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBP1 HKST-UBA02 {ECO:0000313|EMBL:MCB1151607.1}; RA Zhang T.; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:MCB1151607.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBP1 HKST-UBA02 {ECO:0000313|EMBL:MCB1151607.1}; RX PubMed=34615557; RA Wang Y., Ye J., Ju F., Liu L., Boyd J.A., Deng Y., Parks D.H., Jiang X., RA Yin X., Woodcroft B.J., Tyson G.W., Hugenholtz P., Polz M.F., Zhang T.; RT "Successional dynamics and alternative stable states in a saline activated RT sludge microbial community over 9 years."; RL Microbiome 9:0-0(2021). CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21; CC Evidence={ECO:0000256|ARBA:ARBA00001378}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|ARBA:ARBA00001970}; 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:MCB1151607.1}. 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; JAGRNO010000605; MCB1151607.1; -; Genomic_DNA. DR Proteomes; UP000712979; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004096; F:catalase activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:TreeGrafter. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.520.10; -; 1. DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1. DR InterPro; IPR000763; Catalase_peroxidase. DR InterPro; IPR002016; Haem_peroxidase. DR InterPro; IPR010255; Haem_peroxidase_sf. DR InterPro; IPR019794; Peroxidases_AS. DR InterPro; IPR019793; Peroxidases_heam-ligand_BS. DR PANTHER; PTHR30555:SF0; CATALASE-PEROXIDASE; 1. DR PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1. DR Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00460; BPEROXIDASE. DR PRINTS; PR00458; PEROXIDASE. DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1. DR PROSITE; PS00435; PEROXIDASE_1; 1. DR PROSITE; PS00436; PEROXIDASE_2; 1. DR PROSITE; PS50873; PEROXIDASE_4; 1. PE 4: Predicted; KW Heme {ECO:0000256|ARBA:ARBA00022617}; KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..321 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5036916400" FT DOMAIN 145..281 FT /note="Plant heme peroxidase family profile" FT /evidence="ECO:0000259|PROSITE:PS50873" FT NON_TER 321 FT /evidence="ECO:0000313|EMBL:MCB1151607.1" SQ SEQUENCE 321 AA; 34958 MW; 63F286BD63E7C35C CRC64; MTLKHLVAIP LLALALGVAS PALADMPGHG LMTGQANTNE DWWPNRIDLD ILRQNSDLSD PLDDGFDYAA AFSQLDLDAV KKDLQATLTD SQEWWPADWG TYAGLFIRMA WHSAGTYRVT DGRGGSSDGA QRFAPLNSWP DNANLDKARR LLWPVKKKYG RRLSWADLMI LAANVAIESM GLKTFGFAGG REDVWEPEED IYWGKETEWL GDQRYSGDRD LENPLAAVQM GLIYVNPEGP NGQPDPVASG RDVRETFARM AMDDEETVAL VAGGHTFGKA HGAGDPALMG PEPEGAPIEE MGLGWKNGFG TGRGVHTTTS G //