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Database: UniProt
Entry: V8R3Z0_9PSED
LinkDB: V8R3Z0_9PSED
Original site: V8R3Z0_9PSED 
ID   V8R3Z0_9PSED            Unreviewed;       513 AA.
AC   V8R3Z0;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=PMO01_23605 {ECO:0000313|EMBL:ETF05959.1};
OS   Pseudomonas moraviensis R28-S.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1395516 {ECO:0000313|EMBL:ETF05959.1};
RN   [1] {ECO:0000313|EMBL:ETF05959.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R28-S {ECO:0000313|EMBL:ETF05959.1};
RX   PubMed=24558233;
RA   Hunter S.S., Yano H., Loftie-Eaton W., Hughes J., De Gelder L.,
RA   Stragier P., De Vos P., Settles M.L., Top E.M.;
RT   "Draft Genome Sequence of Pseudomonas moraviensis R28-S.";
RL   Genome Announc. 2:e00035-14(2014).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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:ETF05959.1}.
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DR   EMBL; AYMZ01000010; ETF05959.1; -; Genomic_DNA.
DR   RefSeq; WP_016773095.1; NZ_CM002330.1.
DR   AlphaFoldDB; V8R3Z0; -.
DR   PATRIC; fig|1395516.4.peg.4789; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_6; -.
DR   Proteomes; UP000024771; Chromosome.
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   CDD; cd08154; catalase_clade_1; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
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   PIRSF; PIRSF038928; Catalase_clade1-3; 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; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038928-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..513
FT                   /note="Catalase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004772208"
FT   DOMAIN          34..414
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          385..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        153
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         361
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:PIRSR038928-2"
SQ   SEQUENCE   513 AA;  56768 MW;  E2F90983CD66139C CRC64;
     MTSALGLGAF PHRRTLGVLT ASLLTFSVNA APLTRDNGAA VGDNQNSQTA GATGPVLLQD
     VQLIQKLQRF DRERIPERVV HARGTGAHGT FTVTDDLSDL SKAKVFAAGQ STPVFVRFSA
     VVHGNHSPET LRDPRGFATK FYTADGNWDL VGNNFPTFFI RDAIKFPDMV HAFKPDPRTN
     LDDDSRRFDF FSHVPEATRT LTELYSNYGT PASYREMDGN GVHAYKLINA RNEVHYVKFH
     WKSLQGIKNL TPKQVSEVQG QDYSHMTNDL VSNINKGNFP KWDLYVQVLK PQDLSKFDFD
     PLDATKIWPG IAERKVGQMV LNRNPANVFQ ETEQVAMAPA NVVPGIEPSE DRLLQGRVFS
     YADTQMYRLG ANALQLPINA PKTAVNNGNQ DGAMNFGASQ SGVNYQPSRL QPREETPAAR
     YSQSALAGST QQAKIQREQN FKQAGDLYRS YSKQERRDLI DSFGGSLATT DDESKHIILS
     FLYKADPEYG SGVTEVAKGD LSRVKALAAK LTD
//
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