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Database: UniProt/TrEMBL
Entry: S4Y7Q2_SORCE
LinkDB: S4Y7Q2_SORCE
Original site: S4Y7Q2_SORCE 
ID   S4Y7Q2_SORCE            Unreviewed;       724 AA.
AC   S4Y7Q2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   25-OCT-2017, entry version 27.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=SCE1572_33180 {ECO:0000313|EMBL:AGP38918.1};
OS   Sorangium cellulosum So0157-2.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Sorangiineae; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP38918.1, ECO:0000313|Proteomes:UP000014803};
RN   [1] {ECO:0000313|EMBL:AGP38918.1, ECO:0000313|Proteomes:UP000014803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So0157-2 {ECO:0000313|EMBL:AGP38918.1,
RC   ECO:0000313|Proteomes:UP000014803};
RX   PubMed=23812535; DOI=10.1038/srep02101;
RA   Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA   Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT   "Extraordinary expansion of a Sorangium cellulosum genome from an
RT   alkaline milieu.";
RL   Sci. Rep. 3:2101-2101(2013).
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC       {ECO:0000256|RuleBase:RU000498}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038927-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; CP003969; AGP38918.1; -; Genomic_DNA.
DR   RefSeq; WP_020738540.1; NC_021658.1.
DR   EnsemblBacteria; AGP38918; AGP38918; SCE1572_33180.
DR   KEGG; scu:SCE1572_33180; -.
DR   PATRIC; fig|1254432.3.peg.7528; -.
DR   KO; K03781; -.
DR   OrthoDB; POG091H0424; -.
DR   BioCyc; SCEL1254432:G13DY-6590-MONOMER; -.
DR   Proteomes; UP000014803; Chromosome.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
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   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:UP000014803};
KW   Heme {ECO:0000256|RuleBase:RU000498};
KW   Hydrogen peroxide {ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|PIRSR:PIRSR038927-2, ECO:0000256|RuleBase:RU000498};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038927-2,
KW   ECO:0000256|RuleBase:RU000498};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|RuleBase:RU000498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014803}.
FT   DOMAIN       35    423       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     82     82       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    155    155       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       369    369       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
SQ   SEQUENCE   724 AA;  79455 MW;  E0223F2D2785F5D8 CRC64;
     MAEQGEKGAG PEISAHSKID SLEPHREDLA GTVLSTDQGI RIDSTDDSLK AGARGPALLE
     DFHLREKITH FDHERIPERV VHARGSGAHG YFQVYASMAE VTRAAFLQDP SVRTPVFVRF
     STVVGSRGSA DTVRDVRGFA TKFYTKEGNF DLVGNNIPVF FIQDGIKFPD VIHAVKPEPD
     REIPQASSAH DTFWDFISLM PESTHMAMWV LSDRAIPRSF RMMEGFGVHT FRLVNAQGKS
     RFVKFHWKPL LGVHAHVWDE AQELAGRDPD YHRRDLWDAI ERGDYPEYEL GVQIIEEEDE
     FAFDFDLLDA TKIVPEELVP VRRIGKLTLN RNPDNFFAET EQVAFHTANI VPGIDFTDDP
     LLHVRNFSYL DTQLLRLGGP NFPQIPINRP LAPVHNQNRD GFMQQRIKQG RAHYVPNSLA
     GGCPVTASWE TGAFVHYAER VLGLKQRVRS DSFKDHITQA RLFWNSLSVP EKKHLIRAAR
     FELGNVASRD VRERMVARLG EVDTELGRQV AEAIGVAPPA GQPQVPSKGG KAAGKRSVDA
     SPALSMENTV KDTVKSRLVA LLVADGFVVA ELAAVKAALE AAGAHAQVVS TRLGPILGDD
     GSAVEADRSL LTAKSVMFDA VYVPGGRASV AALAASGEAV HFVNEAFKHC KAIGATGDAV
     DLLVATDIQG VALADVQTGA PPLSDKGVVT LRDPAALALF TQELLRAIAQ HRHWDREDIA
     QIPA
//
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