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Database: UniProt/TrEMBL
Entry: F6EH35_HOYSD
LinkDB: F6EH35_HOYSD
Original site: F6EH35_HOYSD 
ID   F6EH35_HOYSD            Unreviewed;       709 AA.
AC   F6EH35;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   28-MAR-2018, entry version 42.
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:AEF39872.1};
GN   OrderedLocusNames=AS9A_1420 {ECO:0000313|EMBL:AEF39872.1};
OS   Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 /
OS   DQS3-9A1) (Amycolicicoccus subflavus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Hoyosella.
OX   NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF39872.1, ECO:0000313|Proteomes:UP000009235};
RN   [1] {ECO:0000313|EMBL:AEF39872.1, ECO:0000313|Proteomes:UP000009235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX   PubMed=21725023; DOI=10.1128/JB.05388-11;
RA   Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA   Wu X.L.;
RT   "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT   actinomycete isolated from crude oil-polluted soil.";
RL   J. Bacteriol. 193:4538-4539(2011).
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; CP002786; AEF39872.1; -; Genomic_DNA.
DR   RefSeq; WP_013806221.1; NC_015564.1.
DR   STRING; 443218.AS9A_1420; -.
DR   EnsemblBacteria; AEF39872; AEF39872; AS9A_1420.
DR   KEGG; asd:AS9A_1420; -.
DR   eggNOG; ENOG4105CH6; Bacteria.
DR   eggNOG; COG0753; LUCA.
DR   KO; K03781; -.
DR   OMA; VMWQMSD; -.
DR   OrthoDB; POG091H0424; -.
DR   Proteomes; UP000009235; 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:UP000009235};
KW   Heme {ECO:0000256|PIRNR:PIRNR038927, 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009235}.
FT   DOMAIN       24    413       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     71     71       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    145    145       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       359    359       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
SQ   SEQUENCE   709 AA;  79276 MW;  83F8263065EF6287 CRC64;
     MERRDSKDRS LDAARTNDDN SWLTTQQGVR VEHTDDSLKA GVRGPTLLED FHAREKITHF
     DHERIPERVV HARGAGAYGY FKAYDTRLRD YTAAEFLTEP KLTTPVFVRF STVAGSRGSA
     DTVRDVRGFA TKFYTKQGNY DLVANNMPVF FIQDGVKFPD FVHAVKPEPA SEIPQAQSAH
     DTFWDFVWLH PESLHMVMWL MSDRALPRSY RMMQGFGVHT FRLVDFEGNG TFVKFHWRPI
     LGSHSLEWAE CQRIAGADPD YNRRDLWDAI EAGQFPEFEL GVQLISELRE HDFDFDLLDP
     TKIVPEEQVP VQPVGRMVLN RNPQNFFAET EQVAFHTANV VPGIDFTNDP LLQARNFSYL
     DTQLIRLGGP NFSQLPINRP VVEVHTNQRD GYGQHTIHTH PTSYTKNSLG NGCPMSMTQQ
     EPPLDVYRHY TQRVEGEVIR RRSESFNDHY SQARLFWNSM KEVEQQHIRD AFCFELSKVS
     SKYVRQRVTE QIAHVDPGLA MGVARKVGVP EPEDFGAALH NDASSALSQV YPVAGFDDAP
     PSIESRRIAA LVCDGVDDTG IRKLASALSA EGALLDLIGP AEGAIRGESG HSVDVSVGLS
     STASVLYDAV IVPGGDIAAL IETNGSAKHF LLEAFKHHKA VAAFGAGVEV LRRNGLTDAE
     TSPVLVADEE GVIVTSHSGQ ELPDEFIRSF IDAVALHRIW NRETSHITA
//
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