ID   KATG_CAUCR              Reviewed;         727 AA.
AC   O31066;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 3.
DT   16-JUN-2009, entry version 74.
DE   RecName: Full=Catalase-peroxidase;
DE            Short=CP;
DE            EC=1.11.1.6;
DE            EC=1.11.1.7;
DE   AltName: Full=Peroxidase/catalase;
GN   Name=katG; OrderedLocusNames=CC_3043;
OS   Caulobacter crescentus (Caulobacter vibrioides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=155892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   MEDLINE=21173698; 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.,
RA   Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J.,
RA   Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J.,
RA   Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L.,
RA   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   MEDLINE=98012985; PubMed=9352936;
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-
CC       spectrum peroxidase activity (By similarity). Important for
CC       stationary phase survival.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer
CC       (By similarity).
CC   -!- SUBUNIT: Homodimer or homotetramer (By similarity).
CC   -!- PTM: The covalent Trp-Tyr-Met adduct is important for the
CC       catalase, but not the peroxidase activity of the enzyme (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily.
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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; -.
DR   HSSP; Q939D2; 1MWV.
DR   PeroxiBase; 2349; CcrCP01.
DR   GeneID; 943888; -.
DR   GenomeReviews; AE005673_GR; CC_3043.
DR   KEGG; ccr:CC_3043; -.
DR   NMPDR; fig|190650.1.peg.3017; -.
DR   TIGR; CC_3043; -.
DR   HOGENOM; O31066; -.
DR   BRENDA; 1.11.1.6; 2191.
DR   GO; GO:0004096; F:catalase activity; IEA:HAMAP.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01961; -; 1.
DR   InterPro; IPR000763; Catalase_proxase.
DR   InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
DR   Pfam; PF00141; peroxidase; 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   Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase.
FT   CHAIN         1    727       Catalase-peroxidase.
FT                                /FTId=PRO_0000055568.
FT   ACT_SITE     96     96       Proton acceptor (By similarity).
FT   METAL       258    258       Iron (heme axial ligand) (By similarity).
FT   SITE         92     92       Transition state stabilizer (By
FT                                similarity).
FT   CROSSLNK     95    217       Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
FT                                (with M-243) (By similarity).
FT   CROSSLNK    217    243       Tryptophyl-tyrosyl-methioninium (Tyr-Met)
FT                                (with W-95) (By similarity).
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
//