ID A0A1V2RI53_9ACTN Unreviewed; 552 AA.
AC A0A1V2RI53;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Catalase {ECO:0000313|EMBL:ONK12129.1};
DE EC=1.11.1.6 {ECO:0000313|EMBL:ONK12129.1};
GN ORFNames=STBA_28680 {ECO:0000313|EMBL:ONK12129.1};
OS Streptomyces sp. MP131-18.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1857892 {ECO:0000313|EMBL:ONK12129.1, ECO:0000313|Proteomes:UP000189065};
RN [1] {ECO:0000313|EMBL:ONK12129.1, ECO:0000313|Proteomes:UP000189065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP131-18 {ECO:0000313|EMBL:ONK12129.1,
RC ECO:0000313|Proteomes:UP000189065};
RA Paulus C., Rebets Y., Tokovenko B., Nadmid S., Terekhova L.P.,
RA Myronovskyi M., Zotchev S.B., Rueckert C., Kalinowski J., Luzhetskyy A.;
RT "New natural products identified by combined genomics-metabolomics
RT profiling of marine Streptomyces sp. MP131-18.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|ARBA:ARBA00002974}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ONK12129.1}.
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DR EMBL; LZNS01000001; ONK12129.1; -; Genomic_DNA.
DR RefSeq; WP_077059599.1; NZ_LZNS01000001.1.
DR AlphaFoldDB; A0A1V2RI53; -.
DR STRING; 1857892.STBA_28680; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000189065; 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; cd08154; catalase_clade_1; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
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:SF23; CATALASE-2; 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; 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 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:0000313|EMBL:ONK12129.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:ONK12129.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189065}.
FT DOMAIN 19..412
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 66
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 354
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 552 AA; 62884 MW; ACCAC6D3FD1D0D8B CRC64;
MTDVSSKGPE PSDERKVLTN RQGHPVYDNQ NQRTVGARGP ATLENYQFLE KISHFDRERV
PERVVHARGV TAYGYFESYG AWGEEPIARH TRAKLFQERG KRTDVAVRFS TVIGGRDSAE
TARDPRGFAV KFYTEEGNWD LVGNNLGVFF IRDAIKFPDV IHALKPDPVS HEQKPARIFD
FMSQTPESMH MLVNLFSPRG IPADYRHMQG FGVNTYKWVN EQGETKLVKY HWMPKQGVRS
MTEADAAAIQ ANELGHATKD LYEAIRRGDH PEWELLVQMM DDHEHPELHF DPLDDTKTWP
EQEFPPRPVG RMVLDRTVDN YFAENEQIAF GTGVLVDGLD FSDDKMLVGR TFSYSDTQRY
RVGANYLQLP VNAAKGAAVR TNQRDGQMAT GVDDSGANPE VNYEPSITGG LREAEYRTTD
DQGPEIRGRV TRKRIPRTND YQQAGQRYLL MEQWEQDDLV HNMVTLLAQC DRPVQERMVW
HFLLVENELG LRVGEGLGIP ADAVRQLPPL ASQTLTEEDE QRLARLGDNP PRDVAGLTMT
HCVPDERHVV RR
//
