ID   CATA_METBF              Reviewed;         505 AA.
AC   O93662; Q46EA1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-NOV-2008, entry version 52.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=kat; OrderedLocusNames=Mbar_A0814;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=99311271; PubMed=10382262; DOI=10.1007/s002030050716;
RA   Shima S., Netrusov A., Sordel M., Wicke M., Hartmann G.C.,
RA   Thauer R.K.;
RT   "Purification, characterization, and primary structure of a
RT   monofunctional catalase from Methanosarcina barkeri.";
RL   Arch. Microbiol. 171:317-323(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen;
CC       serves to protect cells from the toxic effects of hydrogen
CC       peroxide.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; AJ005939; CAA06774.1; -; Genomic_DNA.
DR   EMBL; CP000099; AAZ69791.1; -; Genomic_DNA.
DR   RefSeq; YP_304371.1; -.
DR   HSSP; P04040; 1F4J.
DR   GeneID; 3626836; -.
DR   GenomeReviews; CP000099_GR; Mbar_A0814.
DR   KEGG; mba:Mbar_A0814; -.
DR   NMPDR; fig|269797.3.peg.254; -.
DR   HOGENOM; O93662; -.
DR   BioCyc; MBAR269797:MBAR_A0814-MON; -.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR011614; Catalase_N.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PRINTS; PR00067; CATALASE.
DR   ProDom; PD000510; Catalase; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase.
FT   CHAIN         1    505       Catalase.
FT                                /FTId=PRO_0000085019.
FT   ACT_SITE     58     58       By similarity.
FT   ACT_SITE    131    131       By similarity.
FT   METAL       341    341       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   505 AA;  57066 MW;  2A27C4BEC47BE854 CRC64;
     MGEKNSSKVL TTGFGIPVGD DQNSLTAGNR GPVLMQDVHL LDKLSHFDHE RIPERVVHAK
     GAGAGGYFEV TADVTKYTKA KFLSEIGKRT EVFVRFSTVG GEKGSADSAR DPRGFAVKFY
     TEDGNYDLVG NNTPVFFIRD PLKFPDFIHT QKRNPATNCK DPDMFWDFLS LTPESIHQVT
     ILFSDRGTPA TYRNMNGYSS HTYKWYNEKG EYFWVQYHFK TDQGIKNLTL EEAEKIGGSD
     PDHATRDLYE AIKKGDYPSW TLEMQIMTPE QAEDYRFDIR DITKVWPHGD FPTMKIGKLV
     LNRNPTNYFA EVEQAAFSPA NLVPGIGISP DKMLQGRVFS YHDTHIHRLG PNYNLIPVNA
     PKYSPENSYQ RDGFMRVDAN GGSGPNYWPN SFGGPSPDSV YLEPPFGVSG LAARTLYTHP
     NDDFVQAGNL YRDVMTDYDR ENLVGNIVSH LSAAQKRIQL RQTALFFKAD RDYGSRVAKG
     LELDIKEVER LANMTNEERA RATER
//