KATG_PARL1
ID KATG_PARL1 Reviewed; 721 AA.
AC A7HT94;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Plav_1508;
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
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; CP000774; ABS63127.1; -; Genomic_DNA.
DR RefSeq; WP_012110413.1; NC_009719.1.
DR AlphaFoldDB; A7HT94; -.
DR SMR; A7HT94; -.
DR STRING; 402881.Plav_1508; -.
DR EnsemblBacteria; ABS63127; ABS63127; Plav_1508.
DR KEGG; pla:Plav_1508; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_5; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000006377; 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 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 Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..721
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354854"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 264
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 92
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 95..223
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 249)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 223..249
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 95)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 721 AA; 80298 MW; 15AFA66AD7B670A1 CRC64;
MNTSTSGKCP VMHGSMTTAE RSVTEWWPNA LNLDILHQHD TKPNPMGKDF DYREELKKLD
VAALKKDLQA LMTDSQDWWP ADWGHYGGLM IRMAWHSAGS YRLFDGRGGG GTGNQRFAPL
NSWPDNGNLD KARRLLWPIK KKYGNKLSWA DLYILAGNVA YESMGLKTFG FAFGREDIWH
PEKDVYWGSE KEWLAESVLR YANEEDPESL EAPLGAVHMG LIYVNPQGRD GKPDPLKSAH
DVRVTFKRMA MNDEETAALT AGGHTVGKAH GNGLESNLSA PPEAADIEEQ GFGWVNHKTR
GVGRDTVTSG LEGAWTSKPT TFDMGYFDML FGHEWELKKS PAGAWQWQPI DIKEEDMPVD
VEDPSIRRMP IMTDADMAMK VDPIYREICE RFRKDPEYFK DTFARAWFKL THRDMGPKVR
YVGPEVPAED LIWQDPIPAG NTSYDVGAVK AKIAASGLSV SELVSTAWDS ARTYRGSDMR
GGANGARIRL APQKDWVGNE PERLKKVLSM LEPIAKATGA SLADVIVLAG NVGVEQAAKA
AGFDIAVPFA PGRGDASAEQ TDAESFEALE PLADAYRNFL KRDYELPPEE LMLDRTQLMG
LTGPEMTVLV GGMRVMGTNH GGTRHGVFTD REGALTNDFF VNLTDMGNSW VKNGGHYDVR
DRKTGKTKWT ATRVDLVFGS NSILRAYSEV YAQDDAKEKF VKDFVAAWTK VMNADRFDLK
K
