ID A0A443IH86_9GAMM Unreviewed; 754 AA.
AC A0A443IH86;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 17.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN Name=katE {ECO:0000313|EMBL:RWR03484.1};
GN ORFNames=ED28_00425 {ECO:0000313|EMBL:RWR03484.1};
OS [Pantoea] beijingensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1324864 {ECO:0000313|EMBL:RWR03484.1, ECO:0000313|Proteomes:UP000288794};
RN [1] {ECO:0000313|EMBL:RWR03484.1, ECO:0000313|Proteomes:UP000288794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 27579 {ECO:0000313|EMBL:RWR03484.1,
RC ECO:0000313|Proteomes:UP000288794};
RA Xu F., Liu Y., Wang S., Yin Y., Ma Y., Zhao S., Rong C.;
RT "Draft genome sequence of Pantoea beijingensis strain LMG 27579, an
RT emerging pathogen to Pleurotus eryngii with potential industrial
RT application.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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|PIRNR:PIRNR038927,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC {ECO:0000256|ARBA:ARBA00010660}.
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:RWR03484.1}.
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DR EMBL; JMEE01000001; RWR03484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443IH86; -.
DR Proteomes; UP000288794; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd08155; catalase_clade_2; 1.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW Reference proteome {ECO:0000313|Proteomes:UP000288794}.
FT DOMAIN 81..469
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 201
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 125
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 165
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 214
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 411
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 415
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:PIRSR038927-2"
FT BINDING 422
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 754 AA; 84181 MW; A7454D4C09593FF0 CRC64;
MSKETDNKEL SHNAPATGPE SAKPGLDSLA PADGSHQPAQ HPSAPGKQPT APGSFKTPDT
HNAKIDQLEK NRKGGENFPL TTNQGTRIAN DQNALRAGTR GPTLLEDFIL REKITHFDHE
RIPERIVHAR GSAAHGYFQP YRSLTDITKA DFLRDPDEIT PVFVRFSTVQ GGAGSADTVR
DIRGFATKFY TQEGVFDLVG NNTPVFFIQD AHKFPDFVHA VKPEPHNEMP QGQSAHDTFW
DYVSLQPETL HNVIWAMSDR GIPRSYRTME GFGIHTFRMI NAEGKATFVR FHWKPVAGKA
SLLWDESQKL TGRDPDFHRR DLWEAIEAGD FPEYELGVQL IPEEDEFKFD FDLLDATKLI
PEELVPVDLI GKMVLNRNPD NFFAETEQVA FHPGHIVPGL DFSNDPLLQG RLFSYTDTQI
SRLGGPNFHE IPINRPVCPY HNFQRGGMHR QDIDTNPANY EPNSINDNWP RETPPGPHRG
GFESYQERIE GHKVRDRSPS FGEYYSQPRL FWHSQTPIEQ QHIIDAFSFE LGKLSRPYIR
ERVVDHLVRI DISLAHAVAE NLGIALSDEK LHTAPPKDVN GLKKDASLSL YAVPSGNIKG
RQVALLVSDG VKAADVLEIL QSLKDNGVHT KLLAAHMGQI RADDGSVLPI DATFSGLPSL
TFDAVIVPDG NIDALLLSGD ARYYLLEAYK HLKVIGFSGD ARRFKAQFGL AEGELEEGIV
EDDKAEGVFI SEFLSFLAAH RIWSRSQKAL SVPA
//