ID A0A0S9NXU4_9BURK Unreviewed; 709 AA.
AC A0A0S9NXU4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN Name=katE {ECO:0000313|EMBL:KQP50112.1};
GN ORFNames=ASF44_03660 {ECO:0000313|EMBL:KQP50112.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP50112.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP50112.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP50112.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP50112.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP50112.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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|PIRNR:PIRNR038927,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC {ECO:0000256|ARBA:ARBA00010660}.
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:KQP50112.1}.
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DR EMBL; LMNA01000001; KQP50112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S9NXU4; -.
DR STRING; 1736318.ASF44_03660; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000051759; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW Reference proteome {ECO:0000313|Proteomes:UP000051759}.
FT DOMAIN 40..428
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 160
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 84
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 124
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 173
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 370
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 374
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:PIRSR038927-2"
FT BINDING 381
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 709 AA; 76545 MW; 119F3CC25BA72149 CRC64;
MGAAAQGAPN APNTPAAAKA VDKAADLATE TSVDAGQLLT SNQGLKISDN QNSLKAGRRG
PTLLEDQLLR EKIMAFDHER IPERVVHARG AAAHGVFRVY APQDSLTKAR FLNDPALTTP
VFVRFSTVSG SRGSADTARD VRGFATKFYT QEGNYDLVGN NIPVFFIQDA IKFPDLVHAA
KPEADREIPQ ASTAHDTFWD FISLVPESTH MVMWIMSDRA IPRSYRMMEG FGVHSFRMVN
AQGVSRFVKF HWKPLAGVHG LAWDEAQKLA GKDPDFHRRD LADAIDAGHF PEWELGVQVV
EEADATRFGF DLLDATKLIP EELVPVRPIG KMQLNRNPDN YFAETEQVAF HTGNLVPGID
VSDDPLLQGR MFSYLDTQLT RLGGPNFHEI PINRPVCPMH NMNRDGFHRQ TIAKGRINYE
PSSIDGPPIR EVPASQGGFA SFPEAVNGPK VRHRSETFAD HYSQATLFWQ SQTPVEQQHI
VEALQFELAK VAVPAVRVRM LSNLVNVDRE LAARVAQVLG IPVPAASARV GDKRYPPSPK
LSMIARGNPT GIASRQVAFL AADGVDIASL QAMKAALVKA GAGVKVLSTR LGTLAGAAGG
SVPVDHLIVT MPSVVFDAVC VFGGAGSVAQ LQASGDAVHF VREAFKHAKP VAAMSEAADF
LKTAGVLPGA TPPAGVSTGT DLPALTARFI ADMGAHRRWD RAAQQAMAA
//
