KATG_RHIEC
ID KATG_RHIEC Reviewed; 728 AA.
AC Q2JZT8; Q8RMZ6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=RHE_PF00004;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OG Plasmid p42f.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=CE3; PLASMID=p42f;
RX PubMed=12724378; DOI=10.1099/mic.0.25909-0;
RA Del Carmen Vargas M., Encarnacion S., Davalos A., Reyes-Perez A., Mora Y.,
RA Garcia-De Los Santos A., Brom S., Mora J.;
RT "Only one catalase, katG, is detectable in Rhizobium etli, and is encoded
RT along with the regulator OxyR on a plasmid replicon.";
RL Microbiology 149:1165-1176(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. Important for stationary phase survival.
CC {ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:12724378}.
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 -!- INDUCTION: Expression increases from exponential to early- and late-
CC stationary phase. Induced by H(2)O(2). {ECO:0000269|PubMed:12724378}.
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; AF486647; AAL93241.1; -; Genomic_DNA.
DR EMBL; CP000138; ABC93898.1; -; Genomic_DNA.
DR RefSeq; WP_011428316.1; NC_007766.1.
DR AlphaFoldDB; Q2JZT8; -.
DR SMR; Q2JZT8; -.
DR PeroxiBase; 2371; RetCP01_CFN42.
DR PRIDE; Q2JZT8; -.
DR EnsemblBacteria; ABC93898; ABC93898; RHE_PF00004.
DR KEGG; ret:RHE_PF00004; -.
DR HOGENOM; CLU_025424_2_0_5; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000001936; Plasmid p42f.
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 2: Evidence at transcript level;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Plasmid; Reference proteome.
FT CHAIN 1..728
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354882"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 259
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 93
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 96..218
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 244)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 218..244
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 96)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CONFLICT 56..68
FT /note="EFKKLDLDALKKD -> DIQEARSRRAEKG (in Ref. 1;
FT AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="Q -> H (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="Q -> H (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="F -> L (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="R -> C (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="Q -> H (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="E -> N (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="F -> L (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="L -> F (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="V -> L (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="L -> F (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="E -> K (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 598
FT /note="A -> M (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 652..653
FT /note="AT -> GD (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 659..669
FT /note="TGKEGVYEGRD -> PERKGLYRPR (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="V -> R (in Ref. 1; AAL93241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 79871 MW; A4329443428299BE CRC64;
MDNPTDTAGK CPVAHGNKPR GPSNRDWWPN QLNVQILHHN SGRADPLGKD FDYAEEFKKL
DLDALKKDLH ALMTDSQDWW PADFGHYGGL FIRMAWHSAG TYRITDGRGG AGQGQQRFAP
LNSWPDNANL DKARRLLWPI KQKYGNRISW ADLLILTGNV ALESMGFKTF GFAGGRADVW
EPEELYWGPE GTWLGDERYS GERQLAEPLG AVQMGLIYVN PEGPNGNPDP VAAARDIRET
FARMAMNDEE TVALIAGGHT FGKTHGAGDP SFIGAEPEGG AIEDQGLGWK SSFGTGVGKD
AITAGLEVTW SQTPTKWSNY FFENLFAYEW ELTKSPAGAH QWRAKNAEAS IPDAYEPGKK
HVPTMLTTDL SLRFDPIYEK ISRRFLENPD QFADAFARAW FKLTHRDMGP KVRYLGPEVP
AEDLIWQDVI PAVDHPLVDD KDIAELKAKV LATGLTVQEL VSTAWASAST FRGSDKRGGA
NGARIRLAPQ KDWEANQPAQ LAKVLGVLEG IQKDFNAAQT GAKKISLADL IVLAGAAGVE
KAAAAGGNAV SVPLTPGRMD ASEAQTDAHS FAPLEPRIDG FRNYVNGKRL QFMKPEEALV
DRAQLLTLTG PEMTVLVGGL RVLKAGNPEH GVFTSRPETL TNDFFVNLLD VATQWVPATG
KEGVYEGRDR KTGAAKWTGT RVDLIFGSHS QLRAFAEVYG QADAKQKFVK DFVAAWNKVM
NADRFDLV
