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Database: UniProt
Entry: A0A0F3IVG9_9PROT
LinkDB: A0A0F3IVG9_9PROT
Original site: A0A0F3IVG9_9PROT 
ID   A0A0F3IVG9_9PROT        Unreviewed;       480 AA.
AC   A0A0F3IVG9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:KJV10696.1};
GN   ORFNames=VZ95_03115 {ECO:0000313|EMBL:KJV10696.1};
OS   Elstera litoralis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Elstera.
OX   NCBI_TaxID=552518 {ECO:0000313|EMBL:KJV10696.1, ECO:0000313|Proteomes:UP000033774};
RN   [1] {ECO:0000313|EMBL:KJV10696.1, ECO:0000313|Proteomes:UP000033774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dia-1 {ECO:0000313|EMBL:KJV10696.1,
RC   ECO:0000313|Proteomes:UP000033774};
RA   Rahalkar M.C., Dhakephalkar P.K., Pore S.D., Arora P., Kapse N.G.,
RA   Pandit P.S.;
RT   "Draft genome sequence of Elstera litoralis.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000256|ARBA:ARBA00002974}.
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   -!- 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}.
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:KJV10696.1}.
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DR   EMBL; LAJY01000057; KJV10696.1; -; Genomic_DNA.
DR   RefSeq; WP_045774583.1; NZ_LAJY01000057.1.
DR   AlphaFoldDB; A0A0F3IVG9; -.
DR   PATRIC; fig|552518.3.peg.3568; -.
DR   OrthoDB; 9761719at2; -.
DR   Proteomes; UP000033774; 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; 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; 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   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   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033774}.
FT   DOMAIN          8..394
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..23
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   480 AA;  54019 MW;  D2A5B82BA6DC5625 CRC64;
     MSDKPVMTTS AGAPISDNQN SLTAGARGPV LMQDYQLIEK LAHQNRERIP ERVVHAKGWG
     AFGTLTVTHD ISRYTRAKLF GEIGKQTPLL ARFSTVAGEQ GAADAERDVR GFSLKFYTEE
     GNWDLVGNNT PVFFVRDPLK FPDFIHTQKR HPRTNLRSPT AAWDFWSLSP ESLHQVTILM
     SDRGIPVSPR FMDGFGSHTF SFWNNDGERF WVKFHFKTQQ GHKTLTNAEA DAAIGKSRET
     YQEDLFGAIE RQEFPRWRMC VQIMPELDAD KTAYNPFDLT KVWPHGEYPL IDVGVLELNR
     NADNYFAEIE QAAFSPSNIV PGIGFSPDKM LQARIFAYAD AHRYRLGTHY EALPVNAPKC
     PVHHYHKDGA MRFFRNDTGN PDAYYEPNSF GGPTQDPSVA EPPLRLSGDA ARYNHRDGND
     DYTQAGNLFR LLPDDQKQRL FQNIAASIGG VPQAIIDRQL AHFDKADPAY GAGVRKALGL
//
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