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Database: UniProt/TrEMBL
Entry: A4T5Z7_MYCGI
LinkDB: A4T5Z7_MYCGI
Original site: A4T5Z7_MYCGI 
ID   A4T5Z7_MYCGI            Unreviewed;       480 AA.
AC   A4T5Z7;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:ABP43790.1};
DE            EC=1.11.1.6 {ECO:0000313|EMBL:ABP43790.1};
GN   OrderedLocusNames=Mflv_1308 {ECO:0000313|EMBL:ABP43790.1};
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP43790.1};
RN   [1] {ECO:0000313|EMBL:ABP43790.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43790.1};
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABP43790.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43790.1};
RX   PubMed=23469141;
RA   Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT   "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT   Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT   during Pyrene Degradation.";
RL   PLoS ONE 8:E58066-E58066(2013).
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; CP000656; ABP43790.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4T5Z7; -.
DR   STRING; 350054.Mflv_1308; -.
DR   KEGG; mgi:Mflv_1308; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_11; -.
DR   OrthoDB; 3169619at2; -.
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:ABP43790.1};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:ABP43790.1}.
FT   DOMAIN          7..388
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
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   480 AA;  54703 MW;  496965D6F293F432 CRC64;
     MPEKYTTTDS GAPAPSVEHS LTVGSDGPIL LQDHYLIEQM ANFNRERIPE RQPHAKGGGA
     FGQFEVTHDV SRYTKAAFLQ PGITTEMVAR FSTVAGERGS PDTWRDPRGF ALKFYTSEGN
     FDMVGNNTPV FFIRDPMKFQ NFIRSQKRMA ASNLRDHHMQ WDFWTLSPES AHQVTWLMGD
     RGIPKTWRHM NGYSSHTYSW MNAEGEMFWV KYHFKTDQGI EFLTQEDADR LAGEDADYHQ
     RDLFTAIEDG DFPSWTLHVQ IMPFEDAKTY RYNPFDLTKV WPHGDYPLHE VGRMTLNRNV
     VDYHAQMEQA AFEPNNVVPG TGLSPDKMLL ARGFSYSDAH RARLGVNYKQ IPVNEPHVEV
     NAYSKDGAMR IRNSTDPVYT PNSMGGPEVD PKRASEVHWA SDGDMVRQAY ALRADDDDFG
     QAGTLVRDVL TDEQRDRLAH NIIGHVSDGV KEPVLSRVFE YWRNVDPDLG KKVEEGVRGS
//
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