GenomeNet

Database: UniProt
Entry: A0A2A9DMU1_9CORY
LinkDB: A0A2A9DMU1_9CORY
Original site: A0A2A9DMU1_9CORY 
ID   A0A2A9DMU1_9CORY        Unreviewed;       527 AA.
AC   A0A2A9DMU1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:PFG27475.1};
GN   ORFNames=ATK06_0536 {ECO:0000313|EMBL:PFG27475.1};
OS   Corynebacterium renale.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1724 {ECO:0000313|EMBL:PFG27475.1, ECO:0000313|Proteomes:UP000221653};
RN   [1] {ECO:0000313|EMBL:PFG27475.1, ECO:0000313|Proteomes:UP000221653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20688 {ECO:0000313|EMBL:PFG27475.1,
RC   ECO:0000313|Proteomes:UP000221653};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PFG27475.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PDJF01000001; PFG27475.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9DMU1; -.
DR   STRING; 1724.GCA_001044175_00675; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000221653; Unassembled WGS sequence.
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:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
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; 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   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000221653}.
FT   DOMAIN          26..409
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         355
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   527 AA;  59731 MW;  C65B0F5B180BEAD6 CRC64;
     MAHDKNASVE DIATTGMSPD VEGHSRRENG APVPSENISV TAGPQGPTIL NDIHLIEKLS
     HFNRERVPER NPHAKGNGAF GELHITEDVS QYTKAGLFQK GTVTPMVARF STVAGEQGSP
     DTWRDVHGFA LRFFTEDGNY DIVGNNTPTF FLRDAIKFPD FIHSQKRLGK NGLRDADMQW
     DFWTRTPESA HQVTYLMGGR GTPRSERTMN GYGSHTFQWI NEEGTPVWIK YHFISQQGVH
     NFTADEAEEM AGKNADWLRE DLYNAIEAGD FPKWDVYVQV MPFDEAENYR FNPFDLTKTW
     SQKDYPRIKV GYFELNRNPE NFFAQIEQLA LDPSNLVPGI GLSPDRMLMG RIFAYADAQR
     YRIGPNYRHL PINQSRAPRN TYQHEGPMAY YYNSGAKPTY SPNGYGYGAG YLDDGETSSS
     NHTTYGQAED VYVNPDPHGT DLTRAAYVKH AEDDDFGQAG TLYRDVYNDE EKEELANNIV
     GAMNGVSEEV EQRCYWYWTQ VDENLGARVK ELFTKAKEDA KHQANGL
//
DBGET integrated database retrieval system