KATG_GRAFK
ID KATG_GRAFK Reviewed; 750 AA.
AC A0LZM9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=GFO_0850;
OS Gramella forsetii (strain KT0803).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gramella.
OX NCBI_TaxID=411154;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT0803;
RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA Gloeckner F.O.;
RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT reveals adaptations to degradation of polymeric organic matter.";
RL Environ. Microbiol. 8:2201-2213(2006).
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}.
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DR EMBL; CU207366; CAL65824.1; -; Genomic_DNA.
DR RefSeq; WP_011708761.1; NC_008571.1.
DR AlphaFoldDB; A0LZM9; -.
DR SMR; A0LZM9; -.
DR STRING; 411154.GFO_0850; -.
DR PeroxiBase; 6253; GfoCP01.
DR EnsemblBacteria; CAL65824; CAL65824; GFO_0850.
DR KEGG; gfo:GFO_0850; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_10; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000000755; 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; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..750
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354804"
FT ACT_SITE 113
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 276
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 109
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 112..235
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 261)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 235..261
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 112)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 750 AA; 83111 MW; 5D1FB60D78C142B9 CRC64;
MGNNKSGSED NHKVWEVNES SKCPFMGGAL NKTAGKGTSN RDWWPNQLNL NILRQNSSLI
NPMDDGFNYA EAFKSLDLNA VKQDIYDLMT NSQDWWPADY GHYGPFFIRM AWHSAGTYRI
GDGRGGAGSG QQRFAPLNSW PDNANLDKAR LLLWPVKKKY GKNLSWADLL VLAGNCAHES
MGLKMFGFAG GREDVWEPAQ DVYWGAETEW LNNDERYAGE ELENPLGAAH MGLIYVNPEG
HNGNPDPVEA ASYIRETFGR MAMNDYETVA LIAGGHTFGK THGAADAEEY VEAEPAAAGI
ESQGLGWKNT FGTGNGADTI TSGIEGAWTD TPTKWSNKYF DNLFKYDWEC IKGPGGAYQW
QPKDNAGAGT VPDAHDPDKK HAPFMLTTDL SLKMDPEYEK ISRHFYENPD EFADAYSRAW
FKLTHRDMGP IERYLGPEVP KEELLWQDPI PKVDHEIIND SDIASLKNKI LNTGLSVQEL
VTTAWGSAST FRGSDKRGGA NGGRIRLAPQ NGWEVNNPKQ LGKVIDTLEK IQQDFNESQS
GSKKVSIADL IVLAGCVGVE KAAKTAGHEL KVPFSPGRAD ASQEQTDVEA FEPLEPNADG
FRNYFRNRDH VSASAEELLV DRAQLLTLTV PQMTVLLGGM RAMGANYDGS KKGVFTDRPG
QLTNDFFKNI LEMGLTWKSS SDSETEFDGS DRKTGDVKWT GSRADLIFGS NSELRAIAEV
YGTDDVEAKF VKDFVKAWDK VMNLDRYDLK
