ID A0A365TMI0_9GAMM Unreviewed; 733 AA. AC A0A365TMI0; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 05-DEC-2018, entry version 2. 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:RBI66405.1}; GN ORFNames=DQ400_13565 {ECO:0000313|EMBL:RBI66405.1}; OS Halomonas sulfidaeris. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=115553 {ECO:0000313|EMBL:RBI66405.1, ECO:0000313|Proteomes:UP000252204}; RN [1] {ECO:0000313|EMBL:RBI66405.1, ECO:0000313|Proteomes:UP000252204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SST4 {ECO:0000313|EMBL:RBI66405.1, RC ECO:0000313|Proteomes:UP000252204}; RA Abdel-Mageed W.M., Lehri B., Jarmusch S.A., Miranda K., Goodfellow M., RA Jaspars M., Karlyshev A.V.; RT "Whole genome sequencing of four bacterial strains from South Shetland RT trench revealing bio-synthetic gene clusters."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad- CC spectrum peroxidase activity. {ECO:0000256|HAMAP-Rule:MF_01961, CC ECO:0000256|SAAS:SAAS00699576}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; CC EC=1.11.1.21; Evidence={ECO:0000256|HAMAP-Rule:MF_01961, CC 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 ECO:0000256|SAAS:SAAS00699619}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|HAMAP- CC 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- CC Rule:MF_01961}. CC -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is CC important for the catalase, but not the peroxidase activity of the CC enzyme. {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, ECO:0000256|SAAS:SAAS00699595}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01961}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:RBI66405.1}. 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; QNTU01000009; RBI66405.1; -; Genomic_DNA. DR Proteomes; UP000252204; Unassembled WGS sequence. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR HAMAP; MF_01961; Catal_peroxid; 1. DR InterPro; IPR000763; Catalase_peroxidase. DR InterPro; IPR010255; Haem_peroxidase. DR InterPro; IPR002016; Haem_peroxidase_pln/fun/bac. DR InterPro; IPR019794; Peroxidases_AS. 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; PS00436; PEROXIDASE_2; 1. DR PROSITE; PS50873; PEROXIDASE_4; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000252204}; KW Heme {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451, KW ECO:0000256|SAAS:SAAS01096127}; KW Hydrogen peroxide {ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS00699625}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451, KW ECO:0000256|SAAS:SAAS01096128}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS01096116}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS01096123}; KW Peroxidase {ECO:0000256|HAMAP-Rule:MF_01961, KW ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS01096119, KW ECO:0000313|EMBL:RBI66405.1}. FT DOMAIN 103 431 PEROXIDASE_4. {ECO:0000259|PROSITE: FT PS50873}. FT ACT_SITE 95 95 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01961}. FT METAL 265 265 Iron (heme axial ligand). FT {ECO:0000256|HAMAP-Rule:MF_01961}. FT SITE 91 91 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01961}. FT CROSSLNK 224 250 Tryptophyl-tyrosyl-methioninium (Tyr-Met) FT (with Trp-94). {ECO:0000256|HAMAP-Rule: FT MF_01961}. SQ SEQUENCE 733 AA; 81672 MW; 2E34BFF735481CAB CRC64; MSDQKPTRQE WGARTTPRLQ GNEHWWPDQL NLNVLHQKHP DANPFDETFR YSEAFAKLDV DELCADIDAL MTDSQDWWPA DWGHYGPFFI RMSWHAAGTY RALDGRGGGG TGAQRFAPLN SWPDNGNLDK ARRLLWPIKQ KYGEKLSWAD LLVLAGNRAL ETMGFKTFGF GFGRSDIWAP EDDIYWGPEA EWLGDKDERY TGSFEDGSRV LDNPLAAVQM GLIYVNPEGP NGVPDAAKSA MDVRETFARM GMNDRETVAL TVGGHTFGKM HGNGPADAVG GAPEEAKINE MGVGWANKHE TGLGEYTITS GLEGAWTPTP TKWDNTYLET IFSHEWKVKK SPAGANQWEP VEVKDGFWVP DAHVEGKKNP PVMNAADMAM IVDPDYLKIS KEYRENPDVL ADEFARAWYK LLHRDMGPRA RYLGPQVPNE VLVWQDPVPE HEGPLVNDEQ ITALKQAIAN TGLTAKQLVS TAWASACTYR QTDHRGGANG ARIRLEPQVG WDINVRSGVA DVIDQLEKIK NDSDANISLA DMIVLGGNVG VEKAVKAAGY DITIRFIPGR TDATQEMTEV DTHAYLEPRH DAFRNYMQAQ STGIPAEHLM VDRAFMLNLS APQMAALLGG MRAIGANADE NNTDGILTHR PGQLTNDFFV NLIDMGTVWE PTDESEERFV GRDRKSGETK WTASRVDLVY GSNSQLRAIA EEFGASGGER HMIHKFVSGW VKVMENDRFD LHR //