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Database: UniProt
Entry: A1TGG2_MYCVP
LinkDB: A1TGG2_MYCVP
Original site: A1TGG2_MYCVP 
ID   A1TGG2_MYCVP            Unreviewed;       482 AA.
AC   A1TGG2;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:ABM16262.1};
DE            EC=1.11.1.6 {ECO:0000313|EMBL:ABM16262.1};
GN   OrderedLocusNames=Mvan_5493 {ECO:0000313|EMBL:ABM16262.1};
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM16262.1, ECO:0000313|Proteomes:UP000009159};
RN   [1] {ECO:0000313|EMBL:ABM16262.1, ECO:0000313|Proteomes:UP000009159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) 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}.
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DR   EMBL; CP000511; ABM16262.1; -; Genomic_DNA.
DR   RefSeq; WP_011782617.1; NZ_JACKSD010000035.1.
DR   AlphaFoldDB; A1TGG2; -.
DR   STRING; 350058.Mvan_5493; -.
DR   KEGG; mva:Mvan_5493; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_11; -.
DR   Proteomes; UP000009159; 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; 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; 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; 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   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:ABM16262.1};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:ABM16262.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009159}.
FT   DOMAIN          7..388
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         336
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   482 AA;  54658 MW;  547DF08B8D70BD7B CRC64;
     MADKFTTTDA GAPIPSLEHS LTVGPDGPIL LQDHYLIEQM ANFNRERIPE RQPHAKGGGA
     FGQFEVTQDV SGYTKAAFLQ PGAKTDMVAR FSTVAGERGS PDTWRDPRGF ALKFYTSEGN
     FDMVGNNTPV FFMRDPMKFQ NFIRSQKRMQ ATNLRDHHMQ WDFWTLSPES AHQVTWLMGD
     RGIPKTWRHM NGYSSHTYSW LNAADELFWV KYHIKTDQGV DFLTQEDADR LAGEDGDYHQ
     RDLYTAIEDG NFPSWTLHVQ IMPFEDAKTY RFNPFDLTKV WPHGDYPLHE VGRMTLNRNV
     VDYHAQMEQA AFEPNNIVPG TGLSPDKMLL ARGFSYSDAH RARLGVNYKQ IPVNEPQVEV
     NAYSKDGAMR IRNVTDPVYA PNSMGGPHAD PRRASEVHWA SDGDMVRQAY ALRADDDDFG
     QAGTLVREVL DDEARDRLAH NIIGHVSKGV REPVLSRVFE YWRNVDADLG KKVEEGVRNG
     GG
//
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