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Database: UniProt
Entry: Q5H5R9_XANOR
LinkDB: Q5H5R9_XANOR
Original site: Q5H5R9_XANOR 
ID   Q5H5R9_XANOR            Unreviewed;       363 AA.
AC   Q5H5R9;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE            EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN   Name=srpA {ECO:0000313|EMBL:AAW73701.1};
GN   OrderedLocusNames=XOO0447 {ECO:0000313|EMBL:AAW73701.1};
OS   Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=291331 {ECO:0000313|EMBL:AAW73701.1, ECO:0000313|Proteomes:UP000006735};
RN   [1] {ECO:0000313|EMBL:AAW73701.1, ECO:0000313|Proteomes:UP000006735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC10331 / KXO85 {ECO:0000313|Proteomes:UP000006735};
RX   PubMed=15673718; DOI=10.1093/nar/gki206;
RA   Lee B.M., Park Y.J., Park D.S., Kang H.W., Kim J.G., Song E.S., Park I.C.,
RA   Yoon U.H., Hahn J.H., Koo B.S., Lee G.B., Kim H., Park H.S., Yoon K.O.,
RA   Kim J.H., Jung C.H., Koh N.H., Seo J.S., Go S.J.;
RT   "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT   bacterial blight pathogen of rice.";
RL   Nucleic Acids Res. 33:577-586(2005).
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; AE013598; AAW73701.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5H5R9; -.
DR   STRING; 291331.XOO0447; -.
DR   KEGG; xoo:XOO0447; -.
DR   PATRIC; fig|291331.8.peg.497; -.
DR   HOGENOM; CLU_045961_1_0_6; -.
DR   Proteomes; UP000006735; 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:UP000006735};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          23..363
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          343..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        67
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT   BINDING         337
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;  39069 MW;  4B2121B2A0F8F7F3 CRC64;
     MTLPPPSPPR ARSPVLPLLG IAAIAGGVAL AFAWTAGWIG SDRLTAARMT DTIESSGPPH
     PGFRRAHTKG VCVSGHFQSS GKATWLSSAR IFSQPSTPVL GRMSIGGGDP HGPDGQARVR
     SMALLLRSDD GQQWRTAMNS FPFFVVATPA GFQALNVASK PDPATGKPDP EKLAAFGKQY
     PEAAKFQQWA KTAPWSDSWA NTQYNGVNAF RAIAGDGRER YIRWSMRPQT PFKELSAEQR
     KQADGDFLAT DLDARLTQGP LRWDMVLTIA EPGDAVDDPS QPWPDSRKQI VAGTLLIERA
     QPQATGPCRD LNYDPLILPK GLAASNDPIL AARSSVYSQS FNRREREIAD GQGSAATGQG
     ARQ
//
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