KATG_YERPE
ID KATG_YERPE Reviewed; 737 AA.
AC Q9X6B0; Q0WBX3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 152.
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=Antigen 5;
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Flags: Precursor;
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=katY;
GN OrderedLocusNames=YPO3319, y0870, YP_0367;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-31 AND 250-254,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=KIM;
RX PubMed=10322012; DOI=10.1128/jb.181.10.3114-3122.1999;
RA Garcia E., Nedialkov Y.A., Elliott J., Motin V.L., Brubaker R.R.;
RT "Molecular characterization of KatY (antigen 5), a thermoregulated
RT chromosomally encoded catalase-peroxidase of Yersinia pestis.";
RL J. Bacteriol. 181:3114-3122(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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: Homotetramer. {ECO:0000269|PubMed:10322012}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10322012}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAM84455.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS60640.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF135170; AAD37313.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL21910.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84455.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS60640.1; ALT_INIT; Genomic_DNA.
DR PIR; AC0403; AC0403.
DR RefSeq; WP_002209433.1; NZ_WUCM01000060.1.
DR RefSeq; YP_002348215.1; NC_003143.1.
DR AlphaFoldDB; Q9X6B0; -.
DR SMR; Q9X6B0; -.
DR IntAct; Q9X6B0; 8.
DR STRING; 214092.YPO3319; -.
DR PeroxiBase; 2640; YpCP01.
DR PaxDb; Q9X6B0; -.
DR DNASU; 1145817; -.
DR EnsemblBacteria; AAM84455; AAM84455; y0870.
DR EnsemblBacteria; AAS60640; AAS60640; YP_0367.
DR GeneID; 66842768; -.
DR KEGG; ype:YPO3319; -.
DR KEGG; ypk:y0870; -.
DR KEGG; ypm:YP_0367; -.
DR PATRIC; fig|214092.21.peg.3790; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; EEIFWGP; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Periplasm; Peroxidase; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961,
FT ECO:0000269|PubMed:10322012"
FT CHAIN 24..737
FT /note="Catalase-peroxidase"
FT /id="PRO_0000055578"
FT ACT_SITE 103
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 99
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 102..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 102)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 737 AA; 81365 MW; DB870BC41ABD469A CRC64;
MLKKILPVLI TLAIVHNTPT AWAAEAPKTD SFYLPKSLDL SPLRLHNIES NPYGKDFNYA
QQFKTLDLEA VKKDIKTVLT TSQDWWPADY GNYGPFFIRM AWHGAGTYRI YDGRGGADGG
QQRFEPLNSW PDNANLDKAR RLLWPIKKKY GAKISWGDLM VLTGNVALES MGFKTLGFAG
GREDDWQSDL VYWGAGNKML SDNRDKNGKL PKPLAATQMG LIYVNPEGPN GKPDPVAAAK
DIREAFARMA MNDEETVALI AGGHTFGKAH GAASPEKCLG AAPGEAGLEQ QGLGWANKCG
SGNGKDTITS GLEGAWTTDP THFTMQYLSN LYKHEWVLTK SPAGAWQWKP KNAANVVPDA
TDPTKFHPLM MFTTDIALKV DPEYKKITTR FLENPEEFKM AFARAWFKLT HRDMGPAARY
LGDEVPKETF IWQDPLPAAN YKMIDSADIS ELKDKILKTG LSDTKLIKTA WASASTFRGT
DFRGGDNGAR IRLAPQKDWP VNDPAELHSV LAALMEVQNN FNKDRSDGKK VSLSDLIVLG
GNAAIEDAAK KAGYSISIPF TPGRTDASQE ETDVSSFAVL EPTADGFRNY YDAKRNTLSP
IASLIDRANK LELTVPEMTV LIGGLRVLDV NSGGSKAGVL TNTPGQLNNN FFVNLLDMST
KWTKSPKAEG YFDGYDRKTG KLKWTASSVD LVFGSNPELR AVAEVYASDD AKEKFVHDFT
KVWEKVMNLD RFDIKNN
