UniProt: A0A2R7QZ30

Database: UniProt
Entry: A0A2R7QZ30_9MICC

LinkDB:  A0A2R7QZ30_9MICC 
Original site:  A0A2R7QZ30_9MICC

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (14)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (3)   
   SMART (1)   
All databases (21)   

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ID   A0A2R7QZ30_9MICC        Unreviewed;       495 AA.
AC   A0A2R7QZ30;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=DBR22_15190 {ECO:0000313|EMBL:PTT63831.1};
OS   Arthrobacter sp. HMWF013.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=2056849 {ECO:0000313|EMBL:PTT63831.1, ECO:0000313|Proteomes:UP000244718};
RN   [1] {ECO:0000313|EMBL:PTT63831.1, ECO:0000313|Proteomes:UP000244718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMWF013 {ECO:0000313|EMBL:PTT63831.1,
RC   ECO:0000313|Proteomes:UP000244718};
RA   Go L.Y., Mitchell J.A.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|RuleBase:RU000498};
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, 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:PTT63831.1}.
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DR   EMBL; QAIQ01000408; PTT63831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R7QZ30; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000244718; 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; 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:SF9; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000244718}.
FT   DOMAIN          6..389
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         335
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   495 AA;  54464 MW;  5D1CE786AA477626 CRC64;
     MTVISTTQSG APVTSDAHSQ TVGADGAIIL TDHYLIEKLA QFNRERVPER VVHAKGGGAF
     GTFKATSDVS KYTKAAFLQP GVETEMLIRF SSVAGESGSP DTWRDPRGFA VKFYTSEGNY
     DLVGNNTPVF FIRDGIKFPD FIHSQKRLPG THLRDADMQW DFWTLSPESA HQVTWLMGDR
     GLPASWREMQ GYGSHTYQWI NAEGERFWVK YHFKSNQGVK SITGDQAEEL AGSDADFYIR
     DLQENIAAGN FPSWELHVQV MPYEDAKTYR FNPFDLTKVW PHSDYPLIHV GTMELNKNPE
     NYFAQIEQAT FAPSNFVPGI AASPDKMLQA RIFSYADAHR YRVGTNHAQI PVNLPKNQVN
     NYSQDGAGRY HFNAPSVPVY APNSVGGPAA LEPASPAGGW ENDGELTLSA HSLHAEDGDF
     GQAGTLYREV FDDGAKARLL DTITGAVGGV KTPEIKERAI QYWTNVDAEL GAKLRANLGT
     AAAADSDAES ANKIG
//

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