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Database: UniProt
Entry: D2UB97_XANAP
LinkDB: D2UB97_XANAP
Original site: D2UB97_XANAP 
ID   D2UB97_XANAP            Unreviewed;       363 AA.
AC   D2UB97;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE            EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN   OrderedLocusNames=XALc_0265 {ECO:0000313|EMBL:CBA14809.1};
OS   Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA14809.1, ECO:0000313|Proteomes:UP000001890};
RN   [1] {ECO:0000313|EMBL:CBA14809.1, ECO:0000313|Proteomes:UP000001890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX   PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA   Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., Cociancich S.,
RA   Couloux A., Darrasse A., Gouzy J., Jacques M.A., Lauber E., Manceau C.,
RA   Mangenot S., Poussier S., Segurens B., Szurek B., Verdier V., Arlat M.,
RA   Rott P.;
RT   "The complete genome sequence of Xanthomonas albilineans provides new
RT   insights into the reductive genome evolution of the xylem-limited
RT   Xanthomonadaceae.";
RL   BMC Genomics 10:616-616(2009).
CC   -!- FUNCTION: Has an organic peroxide-dependent peroxidase activity.
CC       {ECO:0000256|PIRNR:PIRNR000296}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000296};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|PIRNR:PIRNR000296}.
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DR   EMBL; FP565176; CBA14809.1; -; Genomic_DNA.
DR   RefSeq; WP_012914826.1; NC_013722.1.
DR   AlphaFoldDB; D2UB97; -.
DR   STRING; 380358.XALC_0265; -.
DR   GeneID; 57875573; -.
DR   KEGG; xal:XALC_0265; -.
DR   PATRIC; fig|29447.3.peg.267; -.
DR   eggNOG; COG0753; Bacteria.
DR   OrthoDB; 255727at2; -.
DR   Proteomes; UP000001890; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd08153; srpA_like; 1.
DR   Gene3D; 1.20.1280.120; -; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR024168; Catalase_SrpA-type_pred.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF9; CATALASE; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PIRSF; PIRSF000296; SrpA; 1.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|PIRNR:PIRNR000296, ECO:0000256|PIRSR:PIRSR000296-2};
KW   Iron {ECO:0000256|PIRNR:PIRNR000296, ECO:0000256|PIRSR:PIRSR000296-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000296,
KW   ECO:0000256|PIRSR:PIRSR000296-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000296};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR000296};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001890};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..363
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        66
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT   BINDING         336
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:PIRSR000296-2"
SQ   SEQUENCE   363 AA;  39053 MW;  D7061F5A10486AC6 CRC64;
     MPHPDPTPPQ RPWLALAGIA TIAVALAAAF AWSAGWLGGP QRLTAQHMTD ALEAGGPPHP
     GFRRAHNKGV CVSGHFESNG QGQALSEARV FAQASVPVLG RLSIGGSDPH GADGQARVRS
     MALQLRSDDG QEWRMAMNNF PFFVVATPEG FMAQIQASQP DPATGKPDPA KMAAFLQRYP
     EAHMFQAWAM SAPWSNSWAN TEYNSVNAFR FTAADGSSRY VRWSMRPHTP FVPLSAAQRA
     LVDANFLGED LQTRLAHGPL RWDLVITVAA PGDPIEDPSR SWPPTRQNVV AGTLVLDHAE
     PQATGPCRDL NYDPLILPHG IAGSGDPILA ARSAVYAQSF NRREREIARG QAPDAIGQKG
     TAQ
//
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