ID B5JLB0_9BACT Unreviewed; 489 AA.
AC B5JLB0;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Catalase {ECO:0000313|EMBL:EDY81042.1};
DE EC=1.11.1.6 {ECO:0000313|EMBL:EDY81042.1};
GN ORFNames=VDG1235_659 {ECO:0000313|EMBL:EDY81042.1};
OS Verrucomicrobiae bacterium DG1235.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae.
OX NCBI_TaxID=382464 {ECO:0000313|EMBL:EDY81042.1, ECO:0000313|Proteomes:UP000003839};
RN [1] {ECO:0000313|EMBL:EDY81042.1, ECO:0000313|Proteomes:UP000003839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG1235 {ECO:0000313|EMBL:EDY81042.1,
RC ECO:0000313|Proteomes:UP000003839};
RA Hart M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; DS990592; EDY81042.1; -; Genomic_DNA.
DR AlphaFoldDB; B5JLB0; -.
DR STRING; 382464.VDG1235_659; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_0; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000003839; 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; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR040333; Catalase_3.
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:SF61; 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; 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:EDY81042.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:EDY81042.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003839}.
FT DOMAIN 9..395
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 129
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 339
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 489 AA; 55609 MW; BD444C1F02B00BF2 CRC64;
MSSNNPRLTT SAGNPIADNQ NSLSAGARGP LLMQDYQLIE KLAHQNRERI PERVVHAKGW
GAFGTFTVTH DITKYTCAKV FSEIGKKTEL VSRFSTVAGE LGAADAERDV RGFSLKFYTD
EGNWDVVGNN TPVFFIRDPY KFPDFIHTQK RHPRTNLRSG KAAWDFWSLS PESLHQVTIL
MSDRGIPTAP MYMNGYGSHT YSFWNEAGER YWVKFHFKTQ QGHRHYTNAE AAEVIGQSRE
TYQEDLFGAI EKGEFPKWTM YVQVMPEAEA EKTSYNPFDL TKVWPHGEYP LIEVGEFELN
RNADNYFTDI EMAAYSPSNV VPGIGFSPDK MLQARVFSYA DAHRYRLGTH YEALPVNRPK
SELNHYHKDG AMRFFTNDFG NPDAYYEPNT VEGSAKEDPS VKEPPLRISG DADRYNHREG
NDDYTQPGNL YRIFNDEQKN RLHHNIAEAM DGVPAGIIEK QLNHFHKCDP AYAKGIADAL
GVEFKPSEA
//
