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Database: UniProt
Entry: A0A0Q2LIT4_MYCGO
LinkDB: A0A0Q2LIT4_MYCGO
Original site: A0A0Q2LIT4_MYCGO 
ID   A0A0Q2LIT4_MYCGO        Unreviewed;       482 AA.
AC   A0A0Q2LIT4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:KQH75706.1};
GN   ORFNames=AO501_09225 {ECO:0000313|EMBL:KQH75706.1};
OS   Mycobacterium gordonae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH75706.1, ECO:0000313|Proteomes:UP000051677};
RN   [1] {ECO:0000313|EMBL:KQH75706.1, ECO:0000313|Proteomes:UP000051677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH75706.1,
RC   ECO:0000313|Proteomes:UP000051677};
RA   Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA   Chernousova L.;
RT   "Mycobacterium gordonae draft genome assembly.";
RL   Submitted (OCT-2015) 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:KQH75706.1}.
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DR   EMBL; LKTM01000371; KQH75706.1; -; Genomic_DNA.
DR   RefSeq; WP_055581360.1; NZ_LKTM01000371.1.
DR   AlphaFoldDB; A0A0Q2LIT4; -.
DR   STRING; 1778.A9W97_27155; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000051677; 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   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   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051677}.
FT   DOMAIN          7..388
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  54852 MW;  1404A91CED21D081 CRC64;
     MTERYTTTDG GSPAPSDEQS LTLGPDGPIL LQDHYLIEQM AQFNRERIPE RQPHAKGGGA
     FGHFEVTNDV SKYTRAAVFQ PGTKTDTLIR FSTVAGERGS PDTWRDPRGF ALKFYTSEGN
     FDMVGNNTPV FFIRDPMKFQ HFIRSQKRMQ ATNLRDHTMQ WDFWTLVPES AHQVTWLMGD
     RGIPKTWRHM NGYSSHTYSW INAAGEIFWV KYHFISDQGV DYLTQEDADR LAGEDGDYHQ
     RDLYETIEGG DFPSWTLKMQ IMPFEEAKTY RYNPFDLTKV WPHGDYPLID VGKLTLTRNV
     TDYHTEIEQA AFEPNNIVPG TGLSPDKMLL ARGFSYSDAH RARLGTNYKQ IPVNTPKVEV
     NSYSKDGAMR IKNATDPVYA PNSFGGPHAD PARAAEVRWQ ADGEMIRAAY TLRPDDDDWS
     QAGTLVREVL DDEARDRLAH NIIGHVSKGV KEPVLSRVFE YWRNVDPDLG KKVEEGVRAN
     LG
//
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