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Database: UniProt
Entry: A0A443IH86_9GAMM
LinkDB: A0A443IH86_9GAMM
Original site: A0A443IH86_9GAMM 
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
//
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