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Database: UniProt/TrEMBL
Entry: C7PGE8_CHIPD
LinkDB: C7PGE8_CHIPD
Original site: C7PGE8_CHIPD 
ID   C7PGE8_CHIPD            Unreviewed;       728 AA.
AC   C7PGE8;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   20-JUN-2018, entry version 61.
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   OrderedLocusNames=Cpin_2389 {ECO:0000313|EMBL:ACU59880.1};
OS   Chitinophaga pinensis (strain ATCC 43595 / DSM 2588 / NCIB 11800 / UQM
OS   2034).
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales;
OC   Chitinophagaceae; Chitinophaga.
OX   NCBI_TaxID=485918 {ECO:0000313|EMBL:ACU59880.1, ECO:0000313|Proteomes:UP000002215};
RN   [1] {ECO:0000313|Proteomes:UP000002215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43595 / DSM 2588 / NCIB 11800 / UQM 2034
RC   {ECO:0000313|Proteomes:UP000002215};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Sims D., Meinche L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Chitinophaga pinensis DSM 2588.";
RL   Submitted (AUG-2009) 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; CP001699; ACU59880.1; -; Genomic_DNA.
DR   RefSeq; WP_012790056.1; NC_013132.1.
DR   ProteinModelPortal; C7PGE8; -.
DR   STRING; 485918.Cpin_2389; -.
DR   PeroxiBase; 7256; CHpiKat01.
DR   EnsemblBacteria; ACU59880; ACU59880; Cpin_2389.
DR   KEGG; cpi:Cpin_2389; -.
DR   eggNOG; ENOG4105CH6; Bacteria.
DR   eggNOG; COG0753; LUCA.
DR   HOGENOM; HOG000087851; -.
DR   KO; K03781; -.
DR   OMA; VMWQMSD; -.
DR   OrthoDB; POG091H0424; -.
DR   BioCyc; CPIN485918:G1GFO-2396-MONOMER; -.
DR   Proteomes; UP000002215; 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:UP000002215};
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, ECO:0000313|EMBL:ACU59880.1};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498, ECO:0000313|EMBL:ACU59880.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002215}.
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   728 AA;  81038 MW;  79C513F9D6771749 CRC64;
     MPDKKKTPIP STENKKIAEL SPNKEDSTGQ DLNTNTGVKI SDDHNSLKAG DRGPTLMEDF
     IFREKMTHFD HERIPERVVH ARGSAAHGVF KVYESMEKYT KAGFLTDTSR ETPVFVRFST
     VAGSRGSTDL ARDVRGFAVK FYTDEGIFDL VGNNMPVFFI QDATKFPDLV HAVKPEPHNE
     IPQAASAHDT FWDFISLMPE STHMIMWLMS DRAIPRSYRM MEGFGVHTFR FVNANEESCF
     VKFHWKPLLG VHSVAWDEAQ KISGKDPDFH RRDLWEAIES GNFPEWELGV QIVPEADEHK
     FDFDLLDATK IIPEELVPVQ RIGKLTLNRN PDNFFAETEQ VAYHIGHVVP GIDFTNDPLL
     QGRLFSYTDT QLIRLGGPNF QEIPINRPVV PVHNNQRDGY MRQTINKGRT SYSPNSLGGG
     YPSQVKAADG GFRSYTEKID ARKIRERSRS FFDHYTQATL FFNSQSAPEK QHLIDALRFE
     LGKVDTVAVR QRMIGILTQV DKDLAAQVAY GLGLEVPAGP EQPVNHGVPA DADPAHYEPF
     PPKEPVPDIS LALSMANTVK DSIQTRKIGF LAADGVDAAS VNAAKSALEA AGAVVEIIAP
     HLGEIVAADG SLIPVQKSLL TASSVFYDAL YVPSGPTSSG TLEADADAVH FLNEAYRHCK
     AIAAHADARQ VLEATYFAKK LPEDDSEESA LMEGVVVQED VKKLSKIFIS AIALHRFWER
     EKPRRVPA
//
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