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Database: UniProt
Entry: A0A1X1D7N1_9GAMM
LinkDB: A0A1X1D7N1_9GAMM
Original site: A0A1X1D7N1_9GAMM 
ID   A0A1X1D7N1_9GAMM        Unreviewed;       488 AA.
AC   A0A1X1D7N1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=HA48_13400 {ECO:0000313|EMBL:ORM72674.1};
OS   Pantoea wallisii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=1076551 {ECO:0000313|EMBL:ORM72674.1, ECO:0000313|Proteomes:UP000193104};
RN   [1] {ECO:0000313|EMBL:ORM72674.1, ECO:0000313|Proteomes:UP000193104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26277 {ECO:0000313|EMBL:ORM72674.1,
RC   ECO:0000313|Proteomes:UP000193104};
RX   PubMed=28255640;
RA   Palmer M., Steenkamp E.T., Coetzee M.P., Chan W.Y., van Zyl E.,
RA   De Maayer P., Coutinho T.A., Blom J., Smits T.H., Duffy B., Venter S.N.;
RT   "Phylogenomic resolution of the bacterial genus Pantoea and its
RT   relationship with Erwinia and Tatumella.";
RL   Antonie Van Leeuwenhoek 0:0-0(2017).
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|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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:ORM72674.1}.
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DR   EMBL; MLFS01000037; ORM72674.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1D7N1; -.
DR   STRING; 1076551.HA48_13400; -.
DR   OrthoDB; 9761719at2; -.
DR   Proteomes; UP000193104; 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; 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:SF9; 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          10..391
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        57
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   488 AA;  55514 MW;  E523CD75FA89DFA0 CRC64;
     MSNDDRKPTT TDAGIPVASD EHSLSVGPDG PLMLHDHYLI EQMANFNRER IPERQPHAKG
     SGAFGYFQVT EDVSRYTKAA VFQPGTKTDV VMRFSTVAGE RGSPDTWRDP RGFSIKFYTT
     EGNYDMVGNN TPVFFIRDPM KFQHFIRSQK RRADNNLRDN DMQWDFWTLS PESAHQVTWL
     MGDRGIPKSW RHMNGYSSHT YMWANAAGEK FWVKYHFKTD QGVEFLAQDH ADLLAGQDGD
     YHTRDLFSAI KNGDFPSWTL YMQIMPFAEA ETYRFNPFDL TKVWPHSDYP LIKVGKLMLN
     RNPTDNHAQI EQAAFEPNNL VPGIGLSPDK MLIGRVFAYA DAHRARLGVN YKQIPVNAPQ
     APVHSYSKDG AMRINPVSDP VYAPNSKGGP VADGERYPTD STWEAHGNMV RAPYTLRQDD
     DDFGQANTLV NKVMDDAARE RLVNNVSGHL LNGVEEPVLS RAFDYWRNID QAIGDRIAQR
     VQTERAKR
//
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