(data stored in SCRATCH zone)

SWISSPROT: D6XX69_BACIE

ID   D6XX69_BACIE            Unreviewed;       729 AA.
AC   D6XX69;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=Catalase-peroxidase {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
DE            Short=CP {ECO:0000256|HAMAP-Rule:MF_01961};
DE            EC=1.11.1.21 {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
DE   AltName: Full=Peroxidase/catalase {ECO:0000256|HAMAP-Rule:MF_01961};
GN   Name=katG {ECO:0000256|HAMAP-Rule:MF_01961};
GN   OrderedLocusNames=Bsel_0386 {ECO:0000313|EMBL:ADH97926.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97926.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97926.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-
CC       spectrum peroxidase activity. {ECO:0000256|HAMAP-Rule:MF_01961,
CC       ECO:0000256|SAAS:SAAS00699576}.
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:0000256|HAMAP-Rule:MF_01961,
CC         ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS01122822};
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:0000256|HAMAP-
CC         Rule:MF_01961, ECO:0000256|RuleBase:RU003451,
CC         ECO:0000256|SAAS:SAAS01122785};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01961};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC       {ECO:0000256|HAMAP-Rule:MF_01961};
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01961}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01961,
CC       ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS00699595}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01961}.
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DR   EMBL; CP001791; ADH97926.1; -; Genomic_DNA.
DR   RefSeq; WP_013171355.1; NC_014219.1.
DR   STRING; 439292.Bsel_0386; -.
DR   EnsemblBacteria; ADH97926; ADH97926; Bsel_0386.
DR   KEGG; bse:Bsel_0386; -.
DR   eggNOG; ENOG4105C1X; Bacteria.
DR   eggNOG; COG0376; LUCA.
DR   HOGENOM; HOG000218110; -.
DR   KO; K03782; -.
DR   OMA; ADVWEPE; -.
DR   OrthoDB; 49441at2; -.
DR   BioCyc; BSEL439292:G1GLR-416-MONOMER; -.
DR   Proteomes; UP000000271; 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   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; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 2.
PE   3: Inferred from homology;
DR   PRODOM; D6XX69.
DR   SWISS-2DPAGE; D6XX69.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Heme {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451,
KW   ECO:0000256|SAAS:SAAS01096127};
KW   Hydrogen peroxide {ECO:0000256|HAMAP-Rule:MF_01961,
KW   ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS00699625};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451,
KW   ECO:0000256|SAAS:SAAS01096128};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01961,
KW   ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS01096116};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01961,
KW   ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS01096123};
KW   Peroxidase {ECO:0000256|HAMAP-Rule:MF_01961,
KW   ECO:0000256|RuleBase:RU003451, ECO:0000256|SAAS:SAAS01096119,
KW   ECO:0000313|EMBL:ADH97926.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN      136    413       PEROXIDASE_4. {ECO:0000259|PROSITE:
FT                                PS50873}.
FT   DOMAIN      463    720       PEROXIDASE_4. {ECO:0000259|PROSITE:
FT                                PS50873}.
FT   ACT_SITE    103    103       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01961}.
FT   METAL       267    267       Iron (heme axial ligand).
FT                                {ECO:0000256|HAMAP-Rule:MF_01961}.
FT   SITE         99     99       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01961}.
FT   CROSSLNK    226    252       Tryptophyl-tyrosyl-methioninium (Tyr-Met)
FT                                (with Trp-102). {ECO:0000256|HAMAP-Rule:
FT                                MF_01961}.
SQ   SEQUENCE   729 AA;  81504 MW;  8BBB9E27A93AF0CA CRC64;
     MDEQKKMNSQ GMCPVMHGGA TSPTRGGTAN QEWWPNQLNL DILHQHDKKT NPFDEDFDYK
     EEFKKMDYFA MKEDLKKLMR TSQDWWPADY GHYGPLFIRM SWHAAGTYRT GDGRGGGGTG
     TQRFAPLNSW PDNANLDKAR RLLWPIKQKY GNKISWADLL VLAGNVAIED MGLPTYGFGA
     GREDVWHPEE DIYWGSEDEW LGDNRYEGTR QDLENPLAAV QMGLIYVNPE GPNGEPDPLK
     SGEDIRETFK RMGMNDEETV ALTAGGHTFG KSHGAGDAAH VGPEPEAAPV EEMGLGWKSA
     HGSGKGSDTI TSGIEGAWTP TPTTWDNTYF ELLLGYEWEL VKSPAGAYQW QAIDVKDEHL
     APDAEDPSKK VKTMMTTADM AMKMDPEYRK ISERFYNNPK EFGEVFAKAW YKLLHRDMGP
     KSRYQGPEVP EEDLIWQDPV PAGNYDLTEA DIKELKDAIL NAGLSTSELV KTAWGSAVTF
     RGSDYRGGAN GARIRLEPQK NWEVNEPEQL DKVLKVLEDV KAKSSKDVSL ADLIVLGGTA
     AVEKAAKEAG VDLTVPFTPG RGDASEEQTD AESFDVLEPI ADGFRNYLKK EYAVSAEELL
     VDKAQLLGLS ATEMTALMGG MRSLGANYQG SDLGIFTDKT EELNTDWFRN LVDMNIEWKP
     VDHYVYEGHD RKTGDVVRKA SRVDLAFGSN SMLRAIVEVY AQDDNKEKFV KDFANAWVKI
     MDNDRFDVK
//

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