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Database: UniProt
Entry: A0A1X2A1R1_9MYCO
LinkDB: A0A1X2A1R1_9MYCO
Original site: A0A1X2A1R1_9MYCO 
ID   A0A1X2A1R1_9MYCO        Unreviewed;       482 AA.
AC   A0A1X2A1R1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:ORW34997.1};
GN   ORFNames=AWC17_22915 {ECO:0000313|EMBL:ORW34997.1};
OS   Mycobacterium nebraskense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=244292 {ECO:0000313|EMBL:ORW34997.1, ECO:0000313|Proteomes:UP000193781};
RN   [1] {ECO:0000313|EMBL:ORW34997.1, ECO:0000313|Proteomes:UP000193781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44803 {ECO:0000313|EMBL:ORW34997.1,
RC   ECO:0000313|Proteomes:UP000193781};
RA   Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA   Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA   Olivier J., Enrico T., Nicola S.;
RT   "The new phylogeny of the genus Mycobacterium.";
RL   Submitted (JAN-2016) 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:ORW34997.1}.
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DR   EMBL; LQPH01000011; ORW34997.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2A1R1; -.
DR   STRING; 244292.ABW17_09215; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000193781; 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}.
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   482 AA;  54611 MW;  3B449A2B3A2B6C60 CRC64;
     MTERFTTTDA GIAAPSDDQS LTIGPDGPIL LQDHYLIEQM AQFNRERIPE RQPHAKGGGA
     FGTFEVTNDV SKYTRAAVFQ PGTKTDMLAR FSTVAGERGS PDTWRDPRGF ALKFYTSEGN
     FDLVGNNTPV FFMRDPLKFQ HFIRSQKRMQ ATNLRDHNMQ WDFWTLSPES AHQVTWLMGD
     RGIPKTWRNM NGYSSHTYSW INAAGEIFWV KYHFKTDQGV DFLTQEDADR LAGEDGDYHQ
     RDLYEAIEGG DHPSWTLKMQ IMPYEEARNY RFNPFDLTKV WPHGDYPLID VGKMTLNRNV
     TDYHTEIEQA AFEPNNTVPG TGFSPDKMLQ ARGFSYSDAH RARLGTNYRQ IPVNTPKVEV
     NSYSKDGAMR VKNVSDPVYA PNSYGGPHAD PARAAEVRWH ADGGMVRAAY TLHAEDDDWG
     QAGTMVRDVL DDAARDRLAH NIIGHVSKGV KEPVLSRVFE YWRNVDPDLG KLVEEGVRAN
     GG
//
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