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Database: UniProt/TrEMBL
Entry: Q9EWJ4_STRCO
LinkDB: Q9EWJ4_STRCO
Original site: Q9EWJ4_STRCO 
ID   Q9EWJ4_STRCO            Unreviewed;       506 AA.
AC   Q9EWJ4;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 133.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   Name=katA2 {ECO:0000313|EMBL:CAC16511.1};
GN   OrderedLocusNames=SCO7590 {ECO:0000313|EMBL:CAC16511.1};
GN   ORFNames=SC7H9.02c {ECO:0000313|EMBL:CAC16511.1};
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226 {ECO:0000313|EMBL:CAC16511.1, ECO:0000313|Proteomes:UP000001973};
RN   [1] {ECO:0000313|EMBL:CAC16511.1, ECO:0000313|Proteomes:UP000001973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145
RC   {ECO:0000313|Proteomes:UP000001973};
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA   Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000720,
CC         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|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; AL939132; CAC16511.1; -; Genomic_DNA.
DR   RefSeq; NP_631632.1; NC_003888.3.
DR   RefSeq; WP_003971553.1; NZ_VNID01000005.1.
DR   AlphaFoldDB; Q9EWJ4; -.
DR   SMR; Q9EWJ4; -.
DR   STRING; 100226.gene:17765250; -.
DR   PaxDb; 100226-SCO7590; -.
DR   PATRIC; fig|100226.15.peg.7705; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_11; -.
DR   InParanoid; Q9EWJ4; -.
DR   OMA; NPSWTCY; -.
DR   OrthoDB; 3169619at2; -.
DR   PhylomeDB; Q9EWJ4; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR   CDD; cd08156; catalase_clade_3; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 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; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF9; CATALASE; 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; Heme-dependent catalase-like; 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   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038928-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001973}.
FT   DOMAIN          9..390
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         338
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-2"
SQ   SEQUENCE   506 AA;  57336 MW;  0A92CD16B6521869 CRC64;
     MTDTPPATTT DSGAPAESDE HSLTAGPAGP VLLQDAYLIE QMAQFNRERI PERQPHAKGS
     GAFGHFEVTH DVSAYTKAAV FQPGTRTDLV ARFSTVAGER GSPDTWRDPR GFAVKFYTSQ
     GNYDMVGNNT PVFFVKDPMK FQHFIRSQKR RADSNLRDHD MQWDFWTLSP ESAHQVTWLM
     GDRGIPRTWR HMNGYTSHTY MWINASGERF WVKYHFKTDQ GIEYFTQHEA DQMAAADTDY
     HMRDLFEHIR DGDFPSWTLH VQVMPYEEAA GYRFNPFDLT KVWPHGDYPL IPVGRMTLER
     NPTDNHAEIE QAAFQPNNLV PGIGPSPDRM LLARLFSYAD AHRYRIGANY QQLPVNAPVV
     DVRTYSKDGA MAYRKTTDPV YAPNSKGGPA ADTEHFGTPP SWETDGSITR TAYVSHAEDD
     DWGQPGTLVR EVMDDAARDR LVDNVVDHLL NEVTEPVLQR AFAYWSNIDR TIGDRIAKGV
     RAKAGEKDFK AAEQRNPARQ AMQDKA
//
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