ID A0A2U8QS91_9FLAO Unreviewed; 739 AA. AC A0A2U8QS91; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 07-OCT-2020, entry version 10. DE RecName: Full=Catalase-peroxidase {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; DE Short=CP {ECO:0000256|HAMAP-Rule:MF_01961}; DE EC=1.11.1.21 {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; DE AltName: Full=Peroxidase/catalase {ECO:0000256|HAMAP-Rule:MF_01961}; GN Name=katG {ECO:0000256|HAMAP-Rule:MF_01961, GN ECO:0000313|EMBL:AWM12724.1}; GN ORFNames=DI487_01785 {ECO:0000313|EMBL:AWM12724.1}; OS Flavobacterium sediminis. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=2201181 {ECO:0000313|EMBL:AWM12724.1, ECO:0000313|Proteomes:UP000245429}; RN [1] {ECO:0000313|EMBL:AWM12724.1, ECO:0000313|Proteomes:UP000245429} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MEBiC07310 {ECO:0000313|EMBL:AWM12724.1, RC ECO:0000313|Proteomes:UP000245429}; RA Baek K.; RT "Flavobacterium sp. MEBiC07310."; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum CC peroxidase activity. {ECO:0000256|HAMAP-Rule:MF_01961}. 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, ECO:0000256|HAMAP- CC Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; CC -!- CATALYTIC ACTIVITY: CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01961}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer. CC {ECO:0000256|HAMAP-Rule:MF_01961}; CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_01961}. CC -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important CC for the catalase, but not the peroxidase activity of the enzyme. CC {ECO:0000256|HAMAP-Rule:MF_01961}. CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01961, CC ECO:0000256|RuleBase:RU003451}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01961}. 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; CP029463; AWM12724.1; -; Genomic_DNA. DR KEGG; fse:DI487_01785; -. DR KO; K03782; -. DR Proteomes; UP000245429; Chromosome. DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR HAMAP; MF_01961; Catal_peroxid; 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; PTHR30555; 1. DR Pfam; PF00141; peroxidase; 2. DR PRINTS; PR00460; BPEROXIDASE. DR PRINTS; PR00458; PEROXIDASE. DR SUPFAM; SSF48113; SSF48113; 2. DR TIGRFAMs; TIGR00198; cat_per_HPI; 1. DR PROSITE; PS00435; PEROXIDASE_1; 1. DR PROSITE; PS00436; PEROXIDASE_2; 1. DR PROSITE; PS50873; PEROXIDASE_4; 1. PE 3: Inferred from homology; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451}; KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324, ECO:0000256|HAMAP- KW Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01961, ECO:0000256|RuleBase:RU003451}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451, ECO:0000313|EMBL:AWM12724.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000245429}. FT DOMAIN 135..414 FT /note="PEROXIDASE_4" FT /evidence="ECO:0000259|PROSITE:PS50873" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 11..25 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 102 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT METAL 270 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT SITE 98 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" FT CROSSLNK 229..255 FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp- FT 101)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961" SQ SEQUENCE 739 AA; 81832 MW; 3B8AA82694DD1659 CRC64; MEHSKNGNGK CPFTGAANSH SAGGGGTRNR DWWPNQLRLG ILRQNSALSN PMGEEFEYAE AFKSLDLDAV KKDLNDLMTD SQEWWPADFG HYGPLFIRMA WHSAGTYRIG DGRGGAGAGQ QRFAPLNSWP DNANLDKARR LLWPIKQKYG KKISWADLMI LAGNVALESM GFKTFGFAGG REDVWEPEED IYWGSEQTWL APSEAPKSRY SGERDLENPL AAVQMGLIYV NPEGPDGNPD PIAAAKDIRE TFARMAMNDE ETVALIAGGH TFGKTHGAGD PALVGAEPEA AGIEEQGLGW KSSFGSGKAS DVITGGPEVT WTQTPTKWSN FFFENLFENE WELTKSPAGA YQWVAKATTE SIPDAFDLTR RHRPTMLTTD LSLRLDPAYE KISRRFYENP DEFADAFARA WFKLTHRDMG PIARYLGPEV PKEDLIWQDP VPTVDHPLVD EKDIESLKNT ILNSGLSIAE LVSTAWASAS TFRGSDKRGG ANGARIRLAP QKYWAVNNPT QLSKVLDSLE NIQKDFNNTQ TNGKKISLAD LIVLGGCAAI EKAAKEAGNV LKVPFTPGRT DATQEQTDVE SFAVLEPIAD GFRNYLKTKF VVSTEELLVD RAQLLTLTAP EMTVLIGGMR MLGTNHEGTQ HGVFTKRQGT LTNDFFVNLL DMGTTWKAID EHEEVFEGRD RSTNELKWTA TRADLIFGSN SELRAIAEVY GSADAKQKFV HDFVAAWNKV MNLDRFDLK //