KATG_CAUVC
ID KATG_CAUVC Reviewed; 727 AA.
AC O31066;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 143.
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=CC_3043;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-484, AND FUNCTION.
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=9352936; DOI=10.1128/jb.179.21.6831-6836.1997;
RA Steinman H.M., Fareed F., Weinstein L.;
RT "Catalase-peroxidase of Caulobacter crescentus: function and role in
RT stationary-phase survival.";
RL J. Bacteriol. 179:6831-6836(1997).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity (By similarity). Important for stationary phase
CC survival. {ECO:0000255|HAMAP-Rule:MF_01961,
CC ECO:0000269|PubMed:9352936}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAC45850.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK25005.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AE005673; AAK25005.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF027168; AAC45850.1; ALT_INIT; Genomic_DNA.
DR PIR; A87626; A87626.
DR PIR; T45480; T45480.
DR RefSeq; NP_421837.1; NC_002696.2.
DR AlphaFoldDB; O31066; -.
DR SMR; O31066; -.
DR STRING; 190650.CC_3043; -.
DR PeroxiBase; 2349; CcrCP01.
DR EnsemblBacteria; AAK25005; AAK25005; CC_3043.
DR KEGG; ccr:CC_3043; -.
DR PATRIC; fig|190650.5.peg.3047; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_5; -.
DR OMA; MILAGNC; -.
DR BRENDA; 1.11.1.21; 1218.
DR Proteomes; UP000001816; 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..727
FT /note="Catalase-peroxidase"
FT /id="PRO_0000055568"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 258
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 92
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 95..217
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 243)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 217..243
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 95)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 727 AA; 79012 MW; 8E6AB7EA0B930516 CRC64;
MDAKVEDNIA GKCPMGHGRG PANRDWWPQS LRLEGLNQHA PRSNPMGEAF DYAEAFKSLD
LDAVVSDLHA LMTDSQEWWP ADFGHYGGLF IRLAWHAAGT YRITDGRGGA GGGQQRFAPL
NSWPDNTNLD KARRLLWPIK QKYGAKLSWA DLYVLVGNVA LESMGFKTFG FAGGRADQWE
PEELYWGPES TWLDDKRYSG ERELDSPLGA VQMGLIYVNP EGPNGNPDPL ASARDIRETF
ARMAMNDEET VALIAGGHTF GKAHGAGDAS LVGVEPEGGA IEAQGFGWAS KHGTGKGPDA
ITGGPEVIWT QTPTRWSNHF FDNLFKYEWE LTQSPAGAKQ WQAKNAPADI PDAFDPNKTH
VPRMLTSDLA LRFDPAYEKI SRRFYENPDQ FADAFARAWF KLTHRDMGPI GRYLGPLVPK
EELIWQDPIP AVDHPLADDK DIAALKAKIL ATGLSASDLV STAWASASTY RQSDKRGGAN
GARIRLAPQK DWAVNNPPVL AKVLAALEGV QKDFNASAGG GKKISLADLI VLGGAAAIEK
AAKDAGTSVT VPFAPGRMDA SAEQTDAHSF EALEPRSDGF RNYRGPGKHY MAPEEALVDR
AQLLGLSGPE LTVLVGGLRV LGANADGSKD GVFTNRPGAL SNDFFVNLLS METTWSPTAA
NAFAGHDRKS SEPRWTATRV DLIFGSHAEL RAFAEVYACA DSQEKFVCDF VTAWNKVMNA
DRLDLAA
