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Database: UniProt/TrEMBL
Entry: A0A0K1E9M8_CHOCO
LinkDB: A0A0K1E9M8_CHOCO
Original site: A0A0K1E9M8_CHOCO 
ID   A0A0K1E9M8_CHOCO        Unreviewed;       720 AA.
AC   A0A0K1E9M8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   20-JUN-2018, entry version 16.
DE   RecName: Full=Catalase {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
GN   Name=katE {ECO:0000313|EMBL:AKT37571.1};
GN   ORFNames=CMC5_017120 {ECO:0000313|EMBL:AKT37571.1};
OS   Chondromyces crocatus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Sorangiineae; Polyangiaceae; Chondromyces.
OX   NCBI_TaxID=52 {ECO:0000313|EMBL:AKT37571.1, ECO:0000313|Proteomes:UP000067626};
RN   [1] {ECO:0000313|EMBL:AKT37571.1, ECO:0000313|Proteomes:UP000067626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cm c5 {ECO:0000313|EMBL:AKT37571.1,
RC   ECO:0000313|Proteomes:UP000067626};
RA   Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT   "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals
RT   a high potential for natural compound synthesis and the genetic basis
RT   for the loss of fruiting body formation.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serves to protect cells from the toxic effects of
CC       hydrogen peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC       {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038927,
CC         ECO:0000256|PIRSR:PIRSR038927-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; CP012159; AKT37571.1; -; Genomic_DNA.
DR   RefSeq; WP_050429919.1; NZ_CP012159.1.
DR   EnsemblBacteria; AKT37571; AKT37571; CMC5_017120.
DR   KEGG; ccro:CMC5_017120; -.
DR   PATRIC; fig|52.7.peg.1838; -.
DR   KO; K03781; -.
DR   Proteomes; UP000067626; Chromosome.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 2.40.180.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR037060; Catalase_core_sf.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   PANTHER; PTHR42821; PTHR42821; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF56634; SSF56634; 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 {ECO:0000313|Proteomes:UP000067626};
KW   Heme {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-3,
KW   ECO:0000256|RuleBase:RU000498};
KW   Hydrogen peroxide {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2,
KW   ECO:0000256|RuleBase:RU000498};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|PIRSR:PIRSR038927-2, ECO:0000256|RuleBase:RU000498};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498, ECO:0000313|EMBL:AKT37571.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067626}.
FT   DOMAIN       33    421       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     80     80       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    153    153       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       367    367       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
FT   BINDING      77     77       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     117    117       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     166    166       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     363    363       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     374    374       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
SQ   SEQUENCE   720 AA;  78395 MW;  704BF4E14570C87B CRC64;
     MSQGNSTSGG APSDKKDAQL EAYRENAGEG FLTTDQGIRV NDTDNSLKVG ERGPTLLEDF
     HFREKIMRFD HERIPERVVH ARGSGAHGHF QVYESLADLT RAKFLQDPAR KTPVFVRFST
     VAGSRGSADT VRDVRGFAVK FYTDEGNFDL VGNNIPVFFI QDGIKFPDVI HAAKPEPHNE
     MPQAATAHDS FWDFASLQTE TTHMLMWALS DRAIPRSLRM MEGFGVHTFR LVNAHGRSRF
     VKFHWKPLLG VHSLVWDEAQ KISGKDPDFH RRDLWEAIEK GSYPEYELGL QIVEEDDAEK
     LGIDLLDATK LIPEEVVPVR RVGKLTLTRN PDNFFAETEQ VAFCVSNVVP GIDVTDDPLM
     QARLFSYLDT QITRLGGPNF AQIPINQPVA PVDNHQQDGF HQHRIPRRRA NYTVNSLGGG
     CPHLANLANG GYVHYPERVE GEKIRKRAES FGDHFSQARL FWVSMSAPEK EHIVKAARFE
     LGKVESLEVR QRMVANFVEV DMGLAKMVAE GIGVDVQAAV KFVGKRNTKP AVAGAPSPAL
     SMENTVKGSV ATRKVAALVA DGVSAAELKD VKTALEAAGA QLEVVGPRLG AVKTAEGGSE
     AVTMALPTVA SVLFDAVLIP GGKASVEALL QDGAALHFVN EAFKHYKTVG ATGEGVDLVR
     GAAFAGVALA DAGGKQGQVT SQGVVTSQGA PDLGAFAKAF LQALGQHRHW DRPGAERVPA
//
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