KATG_POLAQ
ID KATG_POLAQ Reviewed; 717 AA.
AC A4T0J1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Pnuc_2044;
OS Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=312153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX PubMed=22675600; DOI=10.4056/sigs.2395367;
RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT "Complete genome sequence of Polynucleobacter necessarius subsp.
RT asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP35255.1; -; Genomic_DNA.
DR RefSeq; WP_011903878.1; NC_009379.1.
DR AlphaFoldDB; A4T0J1; -.
DR SMR; A4T0J1; -.
DR STRING; 312153.Pnuc_2044; -.
DR EnsemblBacteria; ABP35255; ABP35255; Pnuc_2044.
DR GeneID; 31482435; -.
DR KEGG; pnu:Pnuc_2044; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_4; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000000231; 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 Signal.
FT SIGNAL 1..12
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 13..717
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354860"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 262
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 90
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 93..221
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 247)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 221..247
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 93)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 717 AA; 79677 MW; 123162FCD1A2A41B CRC64;
MTSKGMCPVA HGANTEASET PMAWWPKALN LDILHQQDTK TNPMGSSFSY RDELKKLDVG
ALKKDMKDLL TNSQDWWPAD WGHYGGLMIR MAWHSAGSYR IADGRGGAGT GNQRFAPINS
WPDNANLDKA RRLLWPIKKK YGNKISWADL MILAGTIAYE SMGLKTFGFS FGREDIWHPE
KDIYWGSEKE WLQKSGGKGS RYSGERELSN PLAAVMMGLI YVNPEGVDGK PDPLKTAQDM
RVTFARMAMN DEETVALTAG GHTVGKAHGN GNAANLGPAP EAAPIDEQGL GWMNHKTRGI
GRDAVTSGLE GAWTTHPTQW DNGYFNLLLN YDWKLTESPA GAHQYEPINI KEEDKPVDVE
DASIRCMPMM TDADIALKMD PEYRKISERF SKDQAYFSET FAKAWFKLTH RDMGPKARYF
GPDVPKEELI WQDPIPSGPK SYDIDAVKAK IKASGLSMSD MVTTAWDSAR TFRGSDKRGG
ANGARIRLAP QKDWMGNEPE RLARVLAVYE KIGKECGISI ADTIILGGNI GIEQAAKAGG
FDVKVPFTSG RGDAIQAMTD VESFEVLEPL ADGFRNWLKE SYVVTPEELL LDRTQLMGLT
AQEMTVLIGG MRVLGTNYGG SKQGVFTEKE GVLSNDFFVN LTDMNYLWKP TGQNSYDIVE
RNTEKTKWTA TRADLVFGSN SILRAYAEVY AQDDNKEKFV NDFIAAWTKV MNADLFN
