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Database: UniProt/TrEMBL
Entry: A4FGF7_SACEN
LinkDB: A4FGF7_SACEN
Original site: A4FGF7_SACEN 
ID   A4FGF7_SACEN            Unreviewed;       701 AA.
AC   A4FGF7;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   20-JUN-2018, entry version 75.
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:CAM03132.1};
GN   OrderedLocusNames=SACE_3861 {ECO:0000313|EMBL:CAM03132.1};
GN   ORFNames=A8924_4249 {ECO:0000313|EMBL:PFG96837.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM03132.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAM03132.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAM03132.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG96837.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG96837.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) 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; AM420293; CAM03132.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG96837.1; -; Genomic_DNA.
DR   RefSeq; WP_009947893.1; NZ_PDBV01000001.1.
DR   ProteinModelPortal; A4FGF7; -.
DR   STRING; 405948.SeryN2_010100022737; -.
DR   PeroxiBase; 5236; SerKat02.
DR   EnsemblBacteria; CAM03132; CAM03132; SACE_3861.
DR   KEGG; sen:SACE_3861; -.
DR   eggNOG; ENOG4105CH6; Bacteria.
DR   eggNOG; COG0753; LUCA.
DR   HOGENOM; HOG000087851; -.
DR   KO; K03781; -.
DR   OMA; VMWQMSD; -.
DR   OrthoDB; POG091H0424; -.
DR   BioCyc; SERY405948:SACE_RS18720-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
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:CAM03132.1};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498, ECO:0000313|EMBL:CAM03132.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN       25    414       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     72     72       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    146    146       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       360    360       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
FT   BINDING      69     69       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     110    110       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     159    159       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     356    356       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     367    367       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
SQ   SEQUENCE   701 AA;  77636 MW;  464C0F09682AE10F CRC64;
     MASQHRDKNE QLDQVRQDPQ GTHLTTQQGV RVDHTDDSLQ AGERGPTLME DFHAREKITH
     FDHERIPERV VHARGAGAYG HFQPYDRKMA DYTVARFLSD PSQRTPVFVR FSTVAGSRGS
     ADTVRDVRGF ATKFYTSEGN YDLVGNNMPV FFIQDGIKFP DFVHAVKPEP DNEIPQAQSA
     HDTFWDFVSL QPESLHMVMW LMSDRALPRS YRMMQGFGVH TFRLVNAEGK GTFVKFHWKP
     MLGTHSLAWD ECQKAAGKDP DFNRRDLWES IEAGQFPEWE LGVQLVEEER EFDFDFDLLD
     PTKIIPEEQV PVRPVGRLVL DRNPDNFFAE TEQVAFHTAN VVPGIDFTND PLLQARNFSY
     LDTQLIRLGG PNFAQIPVNR PLAEVSNNQR DGHGQQKIHR GRTSYSPNSL AGGCPVVGGG
     GAFSHYQEKV EGHKIRRRSE SFQDHYSQAT LFWNSMAAWE KEHIVDAFRF ELGKVDHHHV
     REAVVEQINH IDHGMAVAVA EGIGVNPPAD EVRPNHGMSS PALSQANAVM DSIATRKIAV
     LVADGVDATE VDQIRRGLSE RGAIPEVLGP RDGSVRGADS SEVTVDRAIP TMSSVLYDGV
     IVPGGEESVR ALASDGMAVH FVSEAYKHAK PVAASDAGLA MLRRAEVSEA RESSGDGVVN
     DAGVVTAAAT GGALPPNFIA EFASVLAKHR MWERDTSAIP A
//
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