ID A0A0C5JWF2_9BURK Unreviewed; 482 AA.
AC A0A0C5JWF2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=UC34_04825 {ECO:0000313|EMBL:AJP56510.1};
OS Pandoraea vervacti.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=656178 {ECO:0000313|EMBL:AJP56510.1, ECO:0000313|Proteomes:UP000035085};
RN [1] {ECO:0000313|Proteomes:UP000035085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS15 {ECO:0000313|Proteomes:UP000035085};
RA Chan K.-G.;
RT "Complete Genome Sequencing of Pandoraea vervacti NS15 sp. nov.";
RL Submitted (FEB-2015) 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 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; CP010897; AJP56510.1; -; Genomic_DNA.
DR RefSeq; WP_044454333.1; NZ_CP010897.2.
DR AlphaFoldDB; A0A0C5JWF2; -.
DR STRING; 656178.UC34_04825; -.
DR KEGG; pve:UC34_04825; -.
DR PATRIC; fig|656178.5.peg.1022; -.
DR HOGENOM; CLU_010645_2_0_4; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000035085; Chromosome.
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; 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: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; 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}.
FT DOMAIN 8..393
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 55
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 482 AA; 54208 MW; 9506B0D58D9ED259 CRC64;
MSDTKKLTTA AGAPVADNQN TQTAGPRGPA LLQDVWLIEK LAHFDREVIP ERRVHAKGSG
AFGKLTITND ITKYTRARVF ESVGKETPVF LRFSTVAGER GAADAERDVR GFALKFYTDE
GNWDLVGNNT PVFFIRDALK FPDFIHTQKR DPKTNMRNPT AAWDFWSRSP ESLHQVTILM
SDRGIPKNYR QQHGFGSHTF SFINAANERF WVKFHFKSMQ GVENITNAEA AQLVGDDRES
HQRDLFEAIE AGNFPRWRMQ VQVMPEADAA TYRFNPFDIT KVWPHGDYPL IDVGVLELNR
NPENYFAEVE QAAFNPGNVV PGIGFSPDRL LQGRLFSYGD TQRYRLGVNH NAIPVNAPKC
PFHHSFHRDG AMRVDGNLGG APNYEPNRYG AFAEQPAYRD PQQAVGAVAD RFDHRDDDDY
YSQPRALFQL FDDGQKARLF GNIAASMQGV PDDVAERQIG HFAKIDPAYA QGVIAARKAL
AK
//
