KATG_PSEA6
ID KATG_PSEA6 Reviewed; 753 AA.
AC Q15UE5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Flags: Precursor;
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Patl_1975;
OS Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=342610;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6c / ATCC BAA-1087;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA Bartlett D., Higgins B.P., Richardson P.;
RT "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
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:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_01961};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|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; CP000388; ABG40493.1; -; Genomic_DNA.
DR RefSeq; WP_011574788.1; NC_008228.1.
DR AlphaFoldDB; Q15UE5; -.
DR SMR; Q15UE5; -.
DR STRING; 342610.Patl_1975; -.
DR PeroxiBase; 2647; PatCP01.
DR EnsemblBacteria; ABG40493; ABG40493; Patl_1975.
DR KEGG; pat:Patl_1975; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; EEIFWGP; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001981; 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; 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; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 40..753
FT /note="Catalase-peroxidase"
FT /id="PRO_5000125426"
FT ACT_SITE 119
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 282
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:0000255|HAMAP-Rule:MF_01961"
FT SITE 115
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 118..241
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 267)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 241..267
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 118)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 753 AA; 83419 MW; 0BDFBA0FF39D79EB CRC64;
MLPRVNKRSN CIAKKTSNRL ISAVSLAIAS LCISQSALAD GMPKTNTFWW PEQLNLQPLR
QNDAKSNPLG GDFNYADAFK TLNLANVKSD IKALLTSSQD WWPADYGHYG PFFVRMAWHS
TGTYRMSDGR GGGAGGQQRF EPLNSWPDNV SLDKARRLLW PIKQKYGRSL SWADLMVLTG
NVAMESMGFT IYGFAGGRED DFEPDLVYWG PEKKWLGGNE RYSGERKLEE PLAAVQMGLI
YVNPEGPNGN HDPISAAADI RDVFARMAMN DEETVALIAG GHTFGKAHGA HKPDECLDPA
PAGATIEEQG LGWKNKCGKG NAEDTITSGL EGAWSVSPTQ WTMQYLDNLF GFEWVETQSP
AGATQWIPKD NAGANLVPDA HVKSKRHAPI MFTTDLALKE DPQYRKIAER FHANPKEFEL
AFSKAWFKLT HRDMGPRARY VGDESPTDDF LWQDPIPSVD YSLIDKRDIQ HLKTKLLDGD
VTPAQLVKTA WAAAASFRAT DMRGGVNGAR IQLAPQKNWE VNNPDELNTV LMFLNKVKKD
FNDGQSGNKQ VSLADLIVLG GAAAIEHAAS KNDFDVEVPF IPGRSDATQA QTEVESFAVL
EPKADGFRNY YAQGNTLSPV EMLVDKANTL DLSVPEMSVL VAGLRVMNIN ADGSDRGVLT
DNPGTLNNDF FVNLLDMSTR WEKAKDQQDL YLGIDRKSNK QRWSASSVDL IFGSNSELRA
VAEVYASDDA HQQFVDDFVN AWTKVMTLDR FDL
