ID   KATG_ARCFU              Reviewed;         741 AA.
AC   O28050;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 68.
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; Synonyms=perA; OrderedLocusNames=AF_2233;
OS   Archaeoglobus fulgidus.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=2234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   MEDLINE=98049343; PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
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-
CC       spectrum peroxidase activity. Displays also NADH oxidase, INH
CC       lyase and isonicotinoyl-NAD synthase activity.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=32 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0);
CC         KM=3.8 mM for H(2)O(2) for the catalase reaction (at pH 7.0);
CC         KM=95 mM for H(2)O(2) for the peroxidase reaction;
CC         KM=16 mM for ABTS for the peroxidase reaction;
CC         Vmax=11760 umol/min/mg enzyme for H(2)O(2) for the catalase
CC         reaction (at pH 5.5-6.0);
CC         Vmax=5500 umol/min/mg enzyme for H(2)O(2) for the catalase
CC         reaction (at pH 7.0);
CC         Vmax=12 umol/min/mg enzyme for ABTS for the peroxidase reaction;
CC       pH dependence:
CC         Optimum pH is 4.5 for the peroxidase reaction;
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE000782; AAB89022.1; -; Genomic_DNA.
DR   PIR; A69529; A69529.
DR   RefSeq; NP_071058.1; -.
DR   HSSP; O59651; 1ITK.
DR   PeroxiBase; 1858; AfCP01.
DR   GeneID; 1485464; -.
DR   GenomeReviews; AE000782_GR; AF_2233.
DR   KEGG; afu:AF2233; -.
DR   NMPDR; fig|224325.1.peg.2219; -.
DR   TIGR; AF_2233; -.
DR   HOGENOM; O28050; -.
DR   OMA; O28050; FEWELTK.
DR   BioCyc; AFUL224325:AF_2233-MON; -.
DR   BRENDA; 1.11.1.6; 7576.
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   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   Pfam; PF00141; peroxidase; 2.
DR   PRINTS; PR00460; BPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
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   1: Evidence at protein level;
KW   Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase.
FT   CHAIN         1    741       Catalase-peroxidase.
FT                                /FTId=PRO_0000055579.
FT   ACT_SITE     87     87       Proton acceptor (By similarity).
FT   METAL       249    249       Iron (heme axial ligand) (By similarity).
FT   SITE         83     83       Transition state stabilizer (By
FT                                similarity).
FT   CROSSLNK     86    208       Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
FT                                (with M-234) (By similarity).
FT   CROSSLNK    208    234       Tryptophyl-tyrosyl-methioninium (Tyr-Met)
FT                                (with W-86) (By similarity).
SQ   SEQUENCE   741 AA;  84854 MW;  A931DF34F050FC63 CRC64;
     MMRQGGVMVG ARKRWITDWW PNRLNLKILR QNLQNPYGED YDYVEEVENL DIDAVIRDLK
     ELMRSSQDWW PADFGHYGPL FIRLAWHSAG SYRIFDGRGG ARDGSIRFPP RINWPDNINL
     DKAIRLLWPI KKKYGRKLSW ADLIILAGTV AMEDMGVKLF GFALGREDIF EPDESPDWGP
     EEEMLTAKRG EKEELERPFA ATEMGLIYVN PEGPGGNPDP LGSAQEIRVA FRRMGMNDEE
     TVALIAGGHA FGKCHGAGPA DYLGPDPSSS PIEMQGLGWK YNYGKGKGSD TFTSGLEVTW
     SPTPTKFGIN YLRILFTYEW ELEKSPAGKN QWVAKDAPEI IPDAHDPNKK HRPRMLTADL
     ALRFDPEFSK IARRFLENPE EFEKAFAIAW YKLTHRDMGP KDCYIGKYVP EETFVWQDPL
     PRRDYELVDE KDVEELKRRI LASGLSLSQL VYFAWASAST YRNSDRRGGA NGARIRLKPM
     SVWEVNHPEE LKKVIAAYEK IQQEFNEGAK GSEKRISIAD LIVLGGIAAV EEAARRAGFS
     VKVPFIPGRV DAQQEHVDEE FYRVIEPFAD GFRNYFRYPE RINERDVYTT PEYFLVDKAN
     LLTLTVPEMV VLIGGMRALG ANYSHSDYGV LTERPGVLSN DFFVNLLDMS VEWRAADDYR
     YTFEGYDRKS GELRWRATRV DLILGHHDEL RAVAEVYGCD DAKEKFVKDF AAVCAKVMHL
     DRFDLWRSNR KLYKEITAGL R
//