ID A0A0W0VJC7_9GAMM Unreviewed; 486 AA.
AC A0A0W0VJC7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN Name=katA {ECO:0000313|EMBL:KTD20225.1};
GN ORFNames=Lisr_1809 {ECO:0000313|EMBL:KTD20225.1};
OS Legionella israelensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=454 {ECO:0000313|EMBL:KTD20225.1, ECO:0000313|Proteomes:UP000054761};
RN [1] {ECO:0000313|EMBL:KTD20225.1, ECO:0000313|Proteomes:UP000054761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bercovier 4 {ECO:0000313|EMBL:KTD20225.1,
RC ECO:0000313|Proteomes:UP000054761};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-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|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:KTD20225.1}.
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DR EMBL; LNYH01000106; KTD20225.1; -; Genomic_DNA.
DR RefSeq; WP_058502142.1; NZ_UGOE01000001.1.
DR AlphaFoldDB; A0A0W0VJC7; -.
DR STRING; 454.Lisr_1809; -.
DR PATRIC; fig|454.4.peg.1968; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000054761; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054761}.
FT DOMAIN 12..393
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 59
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 131
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 341
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 486 AA; 55893 MW; C7C3B84C331179EA CRC64;
MADDYKNKKF TTTDSGIPVP SDEHSLSIGP NGPLLLHDHY LIEQMANFNR ERIPERQPHA
KGGGAFGYFM VTEDVKKYTK ASVFQPGTKT DVLIRFSTVA GERGSPDTWR DPRGFAVKFY
TSEGNFDMVG NNTPVFFVRD PMKFQHFIRS QKRRANNNLR DHDMQWDFWT LSPESAHQVT
WLMGDRGIPK SWRHMNGYSS HTYMWVNAEG EKFWVKYHFK TDQGIEFLTQ EEADKLAGTD
GDYHNRDLFE AIDRGDYPAW TLYMQIMPFK EAETYRFNPF DLTKVWPHKD YPLIKVGQLT
LNRNPRDFHT EIEQAAFEPN NMVPGTGISP DKMLLARVFS YADAHRARLG VNYKQIPVNK
AKCSVHSYSK DGLMRVENIS DPVYAPNSKG GPQADSSRNP EVATWEAHGD FVREAYTLRK
DDDDFGQANT LVRQVLDDAA RDRLVSNVVA HLKNAVSQPV LKRAFEYWKN IDQEIGQRIE
KGVKES
//
