KATG_GEOSL
ID KATG_GEOSL Reviewed; 727 AA.
AC Q74BE1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=GSU2100;
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
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; AE017180; AAR35476.1; -; Genomic_DNA.
DR RefSeq; NP_953149.1; NC_002939.5.
DR RefSeq; WP_010942744.1; NC_002939.5.
DR AlphaFoldDB; Q74BE1; -.
DR SMR; Q74BE1; -.
DR STRING; 243231.GSU2100; -.
DR PeroxiBase; 2439; GsuCP01.
DR EnsemblBacteria; AAR35476; AAR35476; GSU2100.
DR KEGG; gsu:GSU2100; -.
DR PATRIC; fig|243231.5.peg.2138; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_7; -.
DR InParanoid; Q74BE1; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..727
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354802"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 256
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 89
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 92..215
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 241)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 215..241
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 92)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 727 AA; 79894 MW; 87792DD45DAF70F7 CRC64;
MSADNESRTG RRAAGGGTSN RQWWPNQLNL HILHQHSALS NPMGGDFNYA DEFRKLDLAA
VKKDLHALMT DSQEWWPADW GHYGGLFIRM AWHSAGTYRM GDGRGGAGSG SQRLAPLNSW
PDNVNLDKAR RLLWPIKQKY GRKISWADLM ILAGNCALES MGFRIFGFGG GRVDVWEPEE
DIYWGSEDTW LGDKRYSGDR DLENPLAAVQ MGLIYVNPEG PNGEPDPVAS GRDVRETFAR
MAMNDEETVA LVAGGHTFGK CHGAGPATHV GPEPEAAPLE DQGLGWKSTF RSGKGGDAIG
SGLEGAWKPN PTTWDMGYLK VLFKYEWELV KSPAGANQWL AKDVADEDMV VDAHDPSKKR
RPMMTTADLS LRFDPIYEPI ARRYLANPEE FADAFARAWF KLTHRDMGPR SRYLGPDVPA
EELIWQDPVP AVTHQLIDRQ DIAALKGTIL ASGLSIADLV ATAWASASTF RGSDKRGGAN
GARIRLAPQK DWAVNQPARL ATVLQALEGI RQEFNNAQSG GKQVSLADLI VLGGCAAVEQ
AAKKAGHDVT VPFTPGRADA SQEHTDAASF TVLEPVADGF RNYQKAKYAV TAEELLIDRA
QLLTLTAPEM TVLIGGMRVL NANYGQSKHG VFTRQPETLT NDFFVNLLDM GTVWQPTAAD
KDLFEGRDRV SGELKWTGTR VDLIFGSNSQ LRAVAEVYGC ADSQEKFLND FVAAWNKVMN
LDRFDLA
