KATG_KORVE
ID KATG_KORVE Reviewed; 752 AA.
AC Q1IRZ2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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};
GN OrderedLocusNames=Acid345_1356;
OS Koribacter versatilis (strain Ellin345).
OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC Candidatus Koribacter.
OX NCBI_TaxID=204669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin345;
RX PubMed=19201974; DOI=10.1128/aem.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP000360; ABF40358.1; -; Genomic_DNA.
DR RefSeq; WP_011522160.1; NC_008009.1.
DR AlphaFoldDB; Q1IRZ2; -.
DR SMR; Q1IRZ2; -.
DR STRING; 204669.Acid345_1356; -.
DR PRIDE; Q1IRZ2; -.
DR EnsemblBacteria; ABF40358; ABF40358; Acid345_1356.
DR KEGG; aba:Acid345_1356; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_0; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000002432; 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;
KW Reference proteome.
FT CHAIN 1..752
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354709"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 112
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 275
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 108
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 111..234
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 260)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 234..260
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 111)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 752 AA; 82957 MW; A34B0B095FBDC49E CRC64;
MENELVSKVK APVPGNQTNT LNEAKCPVGA HTLAGARSNA NWWPNQLNIN ILHQHSPLSD
PMPEGFNYAE EFKTLDLDAV VKDLRHLMTD SQPWWPADYG HYGPFFIRMA WHSAGTYRIG
DGRGGAGSGE QRFAPLNSWP DNGNLDKARR LLWPIKQKYG RKLSWADLMV LAGNVALESM
GFKTFGFAGG REDVWEPSED IYWGPEGKWL DDKRYSGERD LENPLGAVQM GLIYVNPEGP
NGKPDPAAAA VDIRETFARM AMNDEETVAL IAGGHTFGKT HGAGVPTEYV GPEPEGAGIE
EQGLGWKNKL GHGHGYHTIT SGLEGAWTTN PIKWDNGFFD NLFGYDWELT KSPAGANQWT
PKNGAGKDTV PDAHDKTKRH APFMATTDIS LKVDPIYGPI SKRFHEHPQE FADAFAKAWY
KLTHRDMGPL PRYLGKLVPK EPQVWQDPVP AVDHELVNDS DVAALKAKLL ASGLTVSQLV
TTAWAAASSF RGSDKRGGAN GARIRLTPQK DWEVNQPKEL AKVLPVLEKI QHDFNAQGGK
KKISLADLII LGGCAAVEEA AKKGGHSVKV PFTPGRTDAS QEHTDVKSFS VMEPKADGFR
NYHQKGQPRP AEEMLVDKAQ LLRLTAPEMT ALVGGLRVLG ANYGHSKHGV FTSHPETLTN
DFFVNLLDMN NRWQPSGADG VYEARDRQGD HVKWTATRVD LIFGSHSQLR AFAEVYACND
AKEKFVHDFV AAWTKVMNLD RYDLAKKKAA AN
