(data stored in ACNUC1104 zone)

SWISSPROT: A4F6H7_SACEN

ID   A4F6H7_SACEN            Unreviewed;       484 AA.
AC   A4F6H7;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   Name=katA {ECO:0000313|EMBL:CAL99651.1};
GN   OrderedLocusNames=SACE_0302 {ECO:0000313|EMBL:CAL99651.1};
GN   ORFNames=A8924_0696 {ECO:0000313|EMBL:PFG93454.1};
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:CAL99651.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99651.1, 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:CAL99651.1};
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:PFG93454.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93454.1,
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240;
CC         EC=1.11.1.6; Evidence={ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|RuleBase:RU000498}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AM420293; CAL99651.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93454.1; -; Genomic_DNA.
DR   RefSeq; WP_009946948.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0302; -.
DR   PeroxiBase; 5233; SerKat01.
DR   EnsemblBacteria; CAL99651; CAL99651; SACE_0302.
DR   KEGG; sen:SACE_0302; -.
DR   eggNOG; ENOG4105CH6; Bacteria.
DR   eggNOG; COG0753; LUCA.
DR   HOGENOM; HOG000087852; -.
DR   KO; K03781; -.
DR   OMA; KLAQFNR; -.
DR   OrthoDB; 1584770at2; -.
DR   BioCyc; SERY405948:SACE_RS01475-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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   CDD; cd08156; catalase_clade_3; 1.
DR   Gene3D; 2.40.180.10; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
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   PANTHER; PTHR11465; PTHR11465; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 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;
DR   PRODOM; A4F6H7.
DR   SWISS-2DPAGE; A4F6H7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
KW   Heme {ECO:0000256|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498};
KW   Hydrogen peroxide {ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038928-2,
KW   ECO:0000256|RuleBase:RU000498};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000498,
KW   ECO:0000313|EMBL:CAL99651.1};
KW   Peroxidase {ECO:0000256|RuleBase:RU000498,
KW   ECO:0000313|EMBL:CAL99651.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN        8    389       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     55     55       {ECO:0000256|PIRSR:PIRSR038928-1}.
FT   ACT_SITE    127    127       {ECO:0000256|PIRSR:PIRSR038928-1}.
FT   METAL       337    337       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038928-2}.
SQ   SEQUENCE   484 AA;  54529 MW;  6292648F48542754 CRC64;
     MSSARFTTTN AGIPVGSDDH SLSAGANGPL LLQDHYLIEK NAQFNRERVP ERVVHAKGGG
     AFGFFEVTED VSQFTKAAVF QPGTRTEALI RFSSVAGELG SPDTWRDPRG TAIKFYTSEG
     NYDLVGNNTP VFFIRDAIKF PDFIRSQKRR ADNHLRDHDM QWDFWTNCPE SAHQVTWLMG
     DRGIPKTWRH MNLYGSHTFM WQNAGGEKFW VKYHFKTEQG HDFLTQAEAD QLAGTDADHH
     IRDLWNTIKA GENPEWTLYV QVMPYADAAD YRFNPFDLTK VWPHGDYPLI KVGRFVLNRN
     PENYFAQIEQ AAFEPSNLVP GIGPSPDKML QGRLFSYPDA HRYRIGTNYA ELPVNRPVSE
     VNSYSKDGAM RFSNTQDPVY APNSYGGPHA DTERFADDVA AAGIEQEILR TAYTLRSEDD
     DFGQPGTMVR NVFSDEERAR FVDNVAGHLN GGVSAPVLER ALAYWRNVDK ATGDRIAEKV
     QAAG
//

If you have problems or comments...

PBIL Back to PBIL home page