ID A0A013WWE9_9SPHN Unreviewed; 497 AA.
AC A0A013WWE9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=BF95_18200 {ECO:0000313|EMBL:EXS70468.1};
OS Sphingobium sp. Ant17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1461752 {ECO:0000313|EMBL:EXS70468.1, ECO:0000313|Proteomes:UP000021537};
RN [1] {ECO:0000313|EMBL:EXS70468.1, ECO:0000313|Proteomes:UP000021537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ant17 {ECO:0000313|EMBL:EXS70468.1,
RC ECO:0000313|Proteomes:UP000021537};
RA Adriaenssens E.M., Cowan D.A.;
RT "Draft genome sequence of the aromatic hydrocarbon-degrading bacterium
RT Sphingobium sp. strain Ant17 isolated from Antarctic soil.";
RL Submitted (FEB-2014) 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 ECO:0000256|RuleBase:RU000498};
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, 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:EXS70468.1}.
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DR EMBL; JEMV01000016; EXS70468.1; -; Genomic_DNA.
DR RefSeq; WP_043151045.1; NZ_JEMV01000016.1.
DR AlphaFoldDB; A0A013WWE9; -.
DR STRING; 1461752.BF95_18200; -.
DR PATRIC; fig|1461752.3.peg.2045; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000021537; 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 11..393
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 58
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 130
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 340
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 497 AA; 55366 MW; 3D29B59361902335 CRC64;
MTDRKDERGS TMSTGAPALS DRNSLTVGPD GPILLQDVHF LEQMAHFNRE KVPERQPHAK
GSGAFGIFQT TKDVSAYTKA ALFQPGTTTD MLARFSTVAG EAGSPDTWRD VRGFSLKFYT
DEGNYDLVGN NTPIFFIRDA MKFPHFIRSQ KRLPDSGLRD NHMQWDFWTS NPESAHQVTY
LMGERGLPRT WRNMNGYGSH TYMWINAEGE RFWVKYHFHT NQGMAFFTNA EAATMAGADA
DFHRRDLFEA IARGEHPSWS LSVQVMPYAD ASAYRINPFD LTKTWSHADY PLIPVGTMTL
NRNPENFFAQ IEQAAFSPGN TVPGIGLSPD KMLLGRAFAY NDAQRNRIGT NFHQLPVNQP
KVAVNTYMFD GHMAYHHSGS APVYAPNSGG RSWADETGPV VDGWEADGPM VRSAYPLRAE
DDDFTQPGIM VRDVFNDGQR TKLVDQVAGS LLGGVRSPVL ERAFEYWKSI DADVGHRIEE
TVRGGGAPKP AEGMGEG
//
