(data stored in SCRATCH zone)

SWISSPROT: B4STC2_STRM5

ID   B4STC2_STRM5            Unreviewed;       367 AA.
AC   B4STC2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE            EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_0260 {ECO:0000313|EMBL:ACF49965.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49965.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49965.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49965.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF49965.1; -; Genomic_DNA.
DR   RefSeq; WP_012509796.1; NC_011071.1.
DR   STRING; 391008.Smal_0260; -.
DR   EnsemblBacteria; ACF49965; ACF49965; Smal_0260.
DR   KEGG; smt:Smal_0260; -.
DR   eggNOG; ENOG4107VGR; Bacteria.
DR   eggNOG; COG0753; LUCA.
DR   HOGENOM; HOG000110273; -.
DR   KO; K03781; -.
DR   OMA; KINHTKG; -.
DR   OrthoDB; 1584770at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01320-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0016021; C:integral component of 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   InterPro; IPR018028; Catalase.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR024168; Catalase_SrpA-type_pred.
DR   PANTHER; PTHR11465; PTHR11465; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PIRSF; PIRSF000296; SrpA; 1.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; SSF56634; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4STC2.
DR   SWISS-2DPAGE; B4STC2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     21     46       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       43    364       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     73     73       {ECO:0000256|PIRSR:PIRSR000296-1}.
FT   METAL       343    343       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000296-2}.
SQ   SEQUENCE   367 AA;  40216 MW;  2B9B416AEB4BE328 CRC64;
     MSLFRYTRAG QTPGAPRKHS PLLWIALIAL ILGAVALAFA WLAGWIGGRL TAQRFTDTIE
     ATGPAHPGFR RAHSKGICVS GWFEPSSQAP TLSSARVFSQ QKVPVMGRLS IGGGDPYGAD
     NTARVRSLAV QMVSDDGQEW RMAMNSFPFF AAPNAEAFYE QTRASIPDPA TGKPDPQKMA
     AVLAKYPSAQ AFQQWAKTAP WTSSWADTTF NSVNSFWFTN VQGQKRAVRW RWQPQAPVVE
     MDADTRKKAS VDFLSQELQQ RLASGPVRWN LVVTTAEPGD AIDDPSVPWP ESREQVVAGV
     LSLDRLQSQE QGACGQINFD PLILPSGVRG SDDPILAARS AVYSQSFNRR ERERASGNVE
     QPKEAAR
//

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