ID A0A1X4IXX3_9RHOB Unreviewed; 501 AA.
AC A0A1X4IXX3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Catalase {ECO:0000313|EMBL:OSP55248.1};
GN ORFNames=BV911_08450 {ECO:0000313|EMBL:OSP55248.1};
OS Pseudoruegeria sp. SK021.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoruegeria.
OX NCBI_TaxID=1933035 {ECO:0000313|EMBL:OSP55248.1, ECO:0000313|Proteomes:UP000194129};
RN [1] {ECO:0000313|EMBL:OSP55248.1, ECO:0000313|Proteomes:UP000194129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK021 {ECO:0000313|EMBL:OSP55248.1,
RC ECO:0000313|Proteomes:UP000194129};
RA Pohlner M., Marshall I., Schreiber L., Cypionka H., Engelen B.;
RT "Draft genome sequence of Pseudoruegeria str. SK021, a representative of
RT the marine Rosebacter group, isolated from North Sea sediment.";
RL Submitted (JAN-2017) 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:OSP55248.1}.
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DR EMBL; MTBG01000010; OSP55248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X4IXX3; -.
DR STRING; 1933035.BV911_08450; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000194129; 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:UP000194129}.
FT DOMAIN 8..395
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..501
FT /note="Polar residues"
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 501 AA; 56478 MW; AEEC1E1179E2B1C5 CRC64;
MTDKPRLTTS AGAPVPSNDT SMTAGERGPV LLQDYQLIEK LAHQNRERIP ERVVHAKGWG
AQGTFTVTHD ITKYSKAAIF SEIGKKTEVL SRWSTVAGES GAADTERDVR GFSLKFYTED
GNWDLVGNNT PVFFVRDAYK FPDFIRTQKR HPKTNLRSPE AMFDFWAAQP ECVHQVTILM
SDRGIPTNPM HMNGYGSHTF SFINADGERF WVKFHFKTQQ GHKHYTNQEA ETLIGKTRES
YQEDLYTAID SGEFPKWTLF VQIMPETDAE KVPYNPFDLT KVWPHGDYPL IEVGELEMNR
NPENYFQMVE NAAYSPSNVV PGIGYSPDKM LQARVFSYAD AHRYRLGTHY EMLPANVAKA
AKVQHYHKDG SMRFFTNDFG NADAYYEPNQ HGGPVADPSV AEPPLRINGD AARYTQLDSD
ADYVQPRALF NLFDDDQKKR LFSNYAAAMG PCSAEVKERW YAVLARVHPD YAAGVRAANE
ASDSDVNAIS VTDETPTETG A
//
