ID F0BHY3_9XANT Unreviewed; 392 AA.
AC F0BHY3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Catalase {ECO:0000313|EMBL:EGD07939.1};
DE EC=1.11.1.6 {ECO:0000313|EMBL:EGD07939.1};
GN ORFNames=XVE_3882 {ECO:0000313|EMBL:EGD07939.1};
OS Xanthomonas vesicatoria ATCC 35937.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=925775 {ECO:0000313|EMBL:EGD07939.1, ECO:0000313|Proteomes:UP000003299};
RN [1] {ECO:0000313|EMBL:EGD07939.1, ECO:0000313|Proteomes:UP000003299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35937 {ECO:0000313|EMBL:EGD07939.1,
RC ECO:0000313|Proteomes:UP000003299};
RX PubMed=21396108; DOI=10.1186/1471-2164-12-146;
RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P.,
RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., Preston J.F.,
RA Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., Staskawicz B.J.,
RA Jones J.B.;
RT "Comparative genomics reveals diversity among xanthomonads infecting tomato
RT and pepper.";
RL BMC Genomics 12:146-146(2011).
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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
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:EGD07939.1}.
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DR EMBL; AEQV01000166; EGD07939.1; -; Genomic_DNA.
DR AlphaFoldDB; F0BHY3; -.
DR Proteomes; UP000003299; 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 Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
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:SF23; CATALASE-2; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 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 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EGD07939.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:EGD07939.1}.
FT DOMAIN 1..293
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 263..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 44101 MW; 905087853FEF4517 CRC64;
MHGNHSPETL RDPHGFATKF YTSEGNWDLV GNNFPTFFIR DAIKFPDMVH AFKPDPRTNL
DDDSRRFDFF SHVPESTRTL TLLYSNEGTP AGYRFMDGNG VHAYKLVNAQ GEVHYVKFHW
KTLQGIKNLD PKQVAAVQSK DYSHLTNDLV GAIKKGDYPK WDLYVQVLKP EDLAKFDFDP
LDATKIWPDV PEQKVGQMVL NKNIDNFFQE TEQVAMAPAN LVPGIEPSED RLLQGRIFSY
ADTQLYRIGA NGLSLPVNRP RVAVNNGNQD GQGNIGQTSS GVNYEPSRLE PRPQDTAARY
SELPLSGTTQ QAKITREQNF KQAGELYRSY SKKDRADLVQ SFGESLANTD TESKHLMLSF
LYKADPEYGT GVTRVAKGDL ARVKQLASSL QD
//
