ID   KATG_HALSA              Reviewed;         720 AA.
AC   O73955; Q9HHP5;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 67.
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;
DE   AltName: Full=Hydroperoxidase;
GN   Name=katG; Synonyms=perA; OrderedLocusNames=VNG_6294G;
OS   Halobacterium salinarium (Halobacterium halobium).
OG   Plasmid pNRC200.
OC   Archaea; Euryarchaeota; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=2242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=11702717; DOI=10.3109/10425170109042049;
RA   Long S., Salin M.L.;
RT   "Molecular cloning, sequencing analysis and expression of the
RT   catalase-peroxidase gene from Halobacterium salinarum.";
RL   DNA Seq. 12:39-51(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1; PLASMID=pNRC200;
RX   MEDLINE=20504483; PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M.,
RA   Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J.,
RA   Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A.,
RA   Leithauser B., Keller K., Cruz R., Danson M.J., Hough D.W.,
RA   Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H.,
RA   Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H.,
RA   Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D.,
RA   Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-
CC       spectrum peroxidase 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   -!- 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; AF069761; AAC23534.1; -; Genomic_DNA.
DR   EMBL; AE004438; AAG20931.1; -; Genomic_DNA.
DR   PIR; T44562; T44562.
DR   RefSeq; NP_395796.1; -.
DR   HSSP; O59651; 1ITK.
DR   PeroxiBase; 2441; HAspCP01.
DR   GeneID; 1449179; -.
DR   GenomeReviews; AE004438_GR; VNG_6294G.
DR   KEGG; hal:VNG6294G; -.
DR   NMPDR; fig|64091.1.peg.2480; -.
DR   HOGENOM; O73955; -.
DR   OMA; O73955; FEWELTK.
DR   BioCyc; HSP64091:VNG6294G-MON; -.
DR   BRENDA; 1.11.1.6; 141893.
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   3: Inferred from homology;
KW   Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase; Plasmid.
FT   CHAIN         1    720       Catalase-peroxidase.
FT                                /FTId=PRO_0000055581.
FT   ACT_SITE     83     83       Proton acceptor (By similarity).
FT   METAL       248    248       Iron (heme axial ligand) (By similarity).
FT   SITE         79     79       Transition state stabilizer (By
FT                                similarity).
FT   CROSSLNK     82    207       Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
FT                                (with M-233) (By similarity).
FT   CROSSLNK    207    233       Tryptophyl-tyrosyl-methioninium (Tyr-Met)
FT                                (with W-82) (By similarity).
SQ   SEQUENCE   720 AA;  80477 MW;  FB88823BCD3CB2F9 CRC64;
     MENEDHNFGT SDWWPNQLDL EILDQNSQQV DPYGEDFDYA EAFEDLDLAA VKDDLEEMMT
     DSKDWWPADY GHYGPLFIRM AWHSAGTYRT FDGRGGAAGG RQRLPPVDSW PDNVNLDKAR
     RLLWPIKQKY GRKLSWGDLI ILAGNVALES MGFETYGFAG GRKDDYTPDE AVDWGPEDEW
     ETTSGDRFDA DGSLKWPLGN TVMGLIYVNP EGPNGEPDLE GSAKNIRESF GKMAMNDKET
     VALIAGGHTF GKVHGADDPE ENVGAEPAAA PIEKQGLGWE NEFGEGKGPD TITSGIEGPW
     NTTPTQWDMS YVDNLLEYEW EPEKGPGGAW QWTTKSGELN ESAPGVQDPT DTEDVMMLTT
     DVALKDDPDY REVLETFQEN PREFQQSFSK AWYKLIHRDM GPSERFLGPE VPEETMIWQD
     PLPDADYDLV DDEAVAALKS ELLESELSIP QLVKTAWASA STYRDSDKRG GANGARIRLE
     PQRSWEVNEP EQLEAALSTY EDIQAEFNDA RSDDMRVSLA DLIVLGGNAA IEQAAADAGY
     DVDVPFEPGR TDATPEQTDV ESFEALKPKA DGFRNYLGDD AEREPEELLV DKAELLNLTA
     DDMTVLVGGL RALGVTHGDS ELGIFTDQPG TLTNDFFTTL LDMDYEWEAA SEDREVFELR
     DRETGDVEWT GSRVDLLFGS NTRLRAIAEV YGSDADEELF VQDFVDTWSE VMKLDRFDLE
//