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Database: UniProt/TrEMBL
Entry: I3U840_ADVKW
LinkDB: I3U840_ADVKW
Original site: I3U840_ADVKW 
ID   I3U840_ADVKW            Unreviewed;       367 AA.
AC   I3U840;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE            EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN   OrderedLocusNames=TKWG_02810 {ECO:0000313|EMBL:AFK61178.1};
OS   Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS   (Tetrathiobacter kashmirensis).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae.
OX   NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK61178.1, ECO:0000313|Proteomes:UP000005267};
RN   [1] {ECO:0000313|EMBL:AFK61178.1, ECO:0000313|Proteomes:UP000005267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17095 / LMG 22695 / WT001
RC   {ECO:0000313|Proteomes:UP000005267};
RX   PubMed=21914874; DOI=10.1128/JB.05781-11;
RA   Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT   "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT   Tetrathiobacter kashmirensis.";
RL   J. Bacteriol. 193:5553-5554(2011).
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; CP003555; AFK61178.1; -; Genomic_DNA.
DR   RefSeq; WP_014749269.1; NC_017964.1.
DR   AlphaFoldDB; I3U840; -.
DR   STRING; 1036672.TKWG_02810; -.
DR   KEGG; aka:TKWG_02810; -.
DR   HOGENOM; CLU_045961_1_0_4; -.
DR   OMA; KINHTKG; -.
DR   OrthoDB; 255727at2; -.
DR   Proteomes; UP000005267; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..367
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          342..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT   BINDING         339
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   367 AA;  39783 MW;  D017637D20A8CBA5 CRC64;
     MLEKNETRPS GLTAGQKLIR FTVIGAAVLG LGAAFGYTGG WLAPQRLTAD RIANTFEPGG
     KSHPGFRRNH AKGICVTGHF ESSGAAQTLS STPMFSPDAS IPLVGRLALP GPNPYAPDSS
     VPIRSFALRF SMPDGQQWRT AMNSMPVFPV ATPQSFYEQQ LASAPDPKTG KPDPARIKAF
     FASHPETAQF RKWVKTARPS ASFATEAYYS LNAFVFTNNE GVRQNVRWRV VPLGTPAADD
     ATPEHDQNYL DMDLVQRLSE GPLRWRLIVT VADPGDPSND ATKPWPDSRR QVEAGTIVIE
     KSQAQDHGPC RDINFDPTVL PQGMAISDDP LLPARSSVYA ASVDRRTREG LSRPSPSSSA
     ASSEHSK
//
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