ID A0A1S8D8T0_9PROT Unreviewed; 507 AA.
AC A0A1S8D8T0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Catalase {ECO:0000313|EMBL:ONH84309.1};
DE EC=1.11.1.6 {ECO:0000313|EMBL:SUE39999.1};
GN Name=katA_1 {ECO:0000313|EMBL:SUE39999.1};
GN ORFNames=APZ41_005050 {ECO:0000313|EMBL:ONH84309.1}, NCTC13291_01621
GN {ECO:0000313|EMBL:SUE39999.1};
OS Roseomonas mucosa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Roseomonas.
OX NCBI_TaxID=207340 {ECO:0000313|EMBL:ONH84309.1, ECO:0000313|Proteomes:UP000054844};
RN [1] {ECO:0000313|EMBL:ONH84309.1, ECO:0000313|Proteomes:UP000054844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAVE376 {ECO:0000313|EMBL:ONH84309.1,
RC ECO:0000313|Proteomes:UP000054844};
RA Choudhury M.A., Sidjabat H.E., Wailan A.M., Zhang L., Marsh N.M.,
RA Rickard C.M., Davies M., Mcmillan D.J.;
RT "Draft genome sequence of Roseomonas mucosa strain AU37, isolated from a
RT peripheral intravenous catheter.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SUE39999.1, ECO:0000313|Proteomes:UP000254919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13291 {ECO:0000313|EMBL:SUE39999.1,
RC ECO:0000313|Proteomes:UP000254919};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000720};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329}.
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DR EMBL; LLWF02000009; ONH84309.1; -; Genomic_DNA.
DR EMBL; UGVN01000001; SUE39999.1; -; Genomic_DNA.
DR RefSeq; WP_019462153.1; NZ_UGVN01000001.1.
DR AlphaFoldDB; A0A1S8D8T0; -.
DR STRING; 207340.APZ41_005050; -.
DR GeneID; 76529524; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000054844; Unassembled WGS sequence.
DR Proteomes; UP000254919; Unassembled WGS sequence.
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; cd08156; catalase_clade_3; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR040333; Catalase_3.
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:SF61; CATALASE; 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; 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 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:0000313|EMBL:SUE39999.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:SUE39999.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054844}.
FT DOMAIN 15..399
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 62
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 135
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 345
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 507 AA; 57332 MW; 3FC18A797ABC41BC CRC64;
MTQETRSGAA RPVLTSTAGA PVPDNQNSLT AGPRGPILLE NYQLIEKLAH QNRERIPERV
VHAKGSGAYG TLTVTHDISR YTRAKVFSQL GKKTEVLLRF STVAGERGAA DAERDVRGFA
LKFYTEEGNW DLVGNNTPVF FIRDPMKFPD FIRTQKRHPR TNMRSATAMW DFWSLSPESL
HQVTILFSDR GLPQGYRFMN GYGSHTYSFW NDAGERYWVK FHFKSMQGIR TWTNEEANTV
IAEDRESAQR DLYDAIEQGD FPRWRVCVQI MPEADAERTS YNPFDLTKVW PHGEYPLIDV
GVLELNRNPE HYFAEIEQSS FSPSNIVPGI GFSPDKVLQG RIFAYADAHR YRVGTHYEAL
PVNRPRSQVN TYHADGPMRF DAPRGTDHYY EPNSFNGPVE QPSAKEPPLR INGNADYYNH
RDGNDDYTQP GNLFRLLGAE QQERLFRNIA GAMQGVPREI VARQLGHFRK ADPAYAAGVE
RALDWVHTSP ASAPTTAADV GGQQAAE
//