(data stored in ACNUC7421 zone)

SWISSPROT: KATG_RHOPS

ID   KATG_RHOPS              Reviewed;         732 AA.
AC   Q13EM6;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 75.
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=RPD_0223;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-
CC       spectrum 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,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240;
CC         EC=1.11.1.21; 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-
CC       Rule:MF_01961}.
CC   -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is
CC       important for the catalase, but not the peroxidase activity of the
CC       enzyme. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
DR   EMBL; CP000283; ABE37463.1; -; Genomic_DNA.
DR   RefSeq; WP_011500653.1; NC_007958.1.
DR   SMR; Q13EM6; -.
DR   STRING; 316057.RPD_0223; -.
DR   EnsemblBacteria; ABE37463; ABE37463; RPD_0223.
DR   KEGG; rpd:RPD_0223; -.
DR   eggNOG; ENOG4105C1X; Bacteria.
DR   eggNOG; COG0376; LUCA.
DR   HOGENOM; HOG000218110; -.
DR   KO; K03782; -.
DR   OMA; ADVWEPE; -.
DR   OrthoDB; 49441at2; -.
DR   BioCyc; RPAL316057:RPD_RS01130-MONOMER; -.
DR   Proteomes; UP000001818; 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;
DR   PRODOM; Q13EM6.
DR   SWISS-2DPAGE; Q13EM6.
KW   Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase.
FT   CHAIN         1    732       Catalase-peroxidase.
FT                                /FTId=PRO_0000354895.
FT   ACT_SITE     98     98       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01961}.
FT   METAL       260    260       Iron (heme axial ligand).
FT                                {ECO:0000255|HAMAP-Rule:MF_01961}.
FT   SITE         94     94       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01961}.
FT   CROSSLNK     97    219       Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
FT                                (with M-245). {ECO:0000255|HAMAP-
FT                                Rule:MF_01961}.
FT   CROSSLNK    219    245       Tryptophyl-tyrosyl-methioninium (Tyr-Met)
FT                                (with W-97). {ECO:0000255|HAMAP-
FT                                Rule:MF_01961}.
SQ   SEQUENCE   732 AA;  80620 MW;  0798EE92BEEC9A6F CRC64;
     MDAKTDDQGG KCPFPHGGGS RGHRNRDWWP EQLDINMLHR NSTLSDPLGK AFDYAKEFES
     LDLDAVIKDL HALMTDSQDW WPADFGHYGG LMIRMAWHSA GTYRTTDGRG GAGAGQQRFA
     PLNSWPDNAN LDKARRLLWP IKQKYGNKIS WADLYVLTGN VALESMGFKT FGFAGGRADT
     WEPEELFWGP EGSWLGDERY SGERQLHDAL GAVQMGLIYV NPEGPNGNPD PVAAAKDIRE
     TFARMAMNDE ETVALIAGGH TFGKTHGAGD PSLIGAEPEG GALEDQGLGW KSKFGTGFGA
     DAITGGPEVI WTQTPTQWSN FFFENLFGFE WELDKSPAGA KQWKAKGAEA TVPDPFDPTK
     KRVPTMLTTD LSLRFDPAYE KISRRFFENP DQFADAFARA WFKLTHRDMG PKVRYRGKLV
     PKEDLIWQDP IPPVDHELVS AKDIADLKAR ILASGLSVSQ LVSTAFASAS TYRHSDKRGG
     ANGARIRFAP QKDWEVNQPA DLAQVLGKLE AIQKAFNDAQ SGGKKVSLAD LIVLGGSAAV
     EKAAKDAGTE VEVPFTPGRM DALEEQTDGD SFKVLEPRAD GFRNFIGKRH QFMQPEEALV
     DRAQLLNLTA PEMTVLLGGL RVLGGNVGHD SHGVFTDRPE KLTNDFFVNL LDMKTAWSLS
     ATAEGVYEGR DRKTGDLRWT GTRVDLIFGS HSQLRALAEV YGQSDAQTKF AQDFVAAWTK
     VMNADRFDLA AK
//

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