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
//