KATG_RHOCA
ID KATG_RHOCA Reviewed; 576 AA.
AC P37743;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Catalase-peroxidase;
DE Short=CP;
DE EC=1.11.1.21;
DE AltName: Full=Hydroperoxidase I;
DE Short=HPI;
DE AltName: Full=Peroxidase/catalase;
GN Name=katG; Synonyms=cpeA;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=8508796; DOI=10.1111/j.1432-1033.1993.tb17918.x;
RA Forkl H., Vandekerckhove J., Drews G., Tadros M.H.;
RT "Molecular cloning, sequence analysis and expression of the gene for
RT catalase-peroxidase (cpeA) from the photosynthetic bacterium Rhodobacter
RT capsulatus B10.";
RL Eur. J. Biochem. 214:251-258(1993).
RN [2]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND HEME-BINDING.
RX PubMed=3571290; DOI=10.1016/s0021-9258(18)48325-1;
RA Hochman A., Shemesh A.;
RT "Purification and characterization of a catalase-peroxidase from the
RT photosynthetic bacterium Rhodopseudomonas capsulata.";
RL J. Biol. Chem. 262:6871-6876(1987).
RN [3]
RP FUNCTION.
RX PubMed=1577703; DOI=10.1128/jb.174.10.3386-3391.1992;
RA Hochman A., Figueredo A., Wall J.D.;
RT "Physiological functions of hydroperoxidases in Rhodobacter capsulatus.";
RL J. Bacteriol. 174:3386-3391(1992).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18178143; DOI=10.1016/j.abb.2007.12.008;
RA Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C.;
RT "Comparative study of catalase-peroxidases (KatGs).";
RL Arch. Biochem. Biophys. 471:207-214(2008).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. Also displays NADH oxidase, INH lyase and
CC isonicotinoyl-NAD synthase activities. Important for stationary phase
CC survival. {ECO:0000269|PubMed:1577703}.
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|PROSITE-
CC ProRule:PRU00297};
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 -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per tetramer.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0)
CC {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:3571290};
CC KM=3.7 mM for H(2)O(2) for the catalase reaction (at pH 7.0)
CC {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:3571290};
CC KM=830 mM for H(2)O(2) for the peroxidase reaction
CC {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:3571290};
CC KM=16 mM for ABTS for the peroxidase reaction
CC {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:3571290};
CC Vmax=10510 umol/min/mg enzyme for H(2)O(2) for the catalase reaction
CC (at pH 5.5-6.0) {ECO:0000269|PubMed:18178143,
CC ECO:0000269|PubMed:3571290};
CC Vmax=5100 umol/min/mg enzyme for H(2)O(2) for the catalase reaction
CC (at pH 7.0) {ECO:0000269|PubMed:18178143,
CC ECO:0000269|PubMed:3571290};
CC Vmax=5.9 umol/min/mg enzyme for ABTS for the peroxidase reaction
CC {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:3571290};
CC pH dependence:
CC Optimum pH is 5.0 for the peroxidase reaction and 6-6.5 for the
CC catalase reaction. {ECO:0000269|PubMed:18178143,
CC ECO:0000269|PubMed:3571290};
CC -!- SUBUNIT: Homotetramer.
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:0000250}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000305}.
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DR EMBL; X71420; CAA50552.1; -; Genomic_DNA.
DR PIR; S33327; S33327.
DR AlphaFoldDB; P37743; -.
DR SMR; P37743; -.
DR PeroxiBase; 2442; RcaCP01.
DR GO; GO:0004096; F:catalase activity; IEA:InterPro.
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 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 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; Peroxidase.
FT CHAIN 1..576
FT /note="Catalase-peroxidase"
FT /id="PRO_0000055575"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 265
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|PROSITE-ProRule:PRU00297"
FT SITE 92
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CROSSLNK 95..224
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 250)"
FT /evidence="ECO:0000250"
FT CROSSLNK 224..250
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 95)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 576 AA; 61517 MW; FEA464541CB3B5B5 CRC64;
MDGKDKATGK CPVMHGAMTA AGVSNTSWWP NALNLDILHQ HDTKGNPLNG FDYRAAVKGL
DVGLRADLHA LMTDSQPWWP ADWGHYGGLM IRMAWHAAGS YRAADGRGGG NTGKPARFAP
LNSWPDNVSL DKARRLLWPI KKKYGNAVSW ADLILFAGTV AYESMGLKTF GFGFGREDIW
APEKDVYWGA EKDWLAPSDG RYGDLAKPET MENPLAAVQM GLIYVNPEGV NGQPDPARTA
LHIRETFARM GMNDEETVAL TAGGHTVGKA HGNGDAKALG PDPEAADVTV RALAGRTRIW
AARRRRPSPR GSRAPGPRIR RAGTWAISRC SSGHDWELTK SPAGAWQWKP VTIAEEAKPL
DATDLTTRHD PLMTDADMAM KVDPSTMRSV RSSWPIRPPS TTLSRAPGSS CCIATWGRRR
ATSAPMCPPR IWSAGPGAAG PTGWDVAKVK AQIAASGLSV ADLVATAWDS ARTFRQSDYR
GGANGARIRL APQKDWAGNE PERLAGACGA RTDRGGAGAS VADVIVLAGN LGVEQAAAGV
SRWRCPSPPV AAMRAAMTDG PSLTCWSRCM TASATG
