ID A0A1B8SAC7_9MYCO Unreviewed; 482 AA.
AC A0A1B8SAC7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Catalase {ECO:0000313|EMBL:OBY29632.1};
GN ORFNames=ACT18_22015 {ECO:0000313|EMBL:OBY29632.1};
OS Mycolicibacter kumamotonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=354243 {ECO:0000313|EMBL:OBY29632.1, ECO:0000313|Proteomes:UP000092668};
RN [1] {ECO:0000313|EMBL:OBY29632.1, ECO:0000313|Proteomes:UP000092668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Roo {ECO:0000313|EMBL:OBY29632.1,
RC ECO:0000313|Proteomes:UP000092668};
RA Greninger A.L., Cunningham G., Miller S.;
RT "Genome sequence of Mycobacterium kumamotonense strain Roo.";
RL Submitted (JUN-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:OBY29632.1}.
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DR EMBL; LFOE01000060; OBY29632.1; -; Genomic_DNA.
DR RefSeq; WP_065289556.1; NZ_LFOE01000060.1.
DR AlphaFoldDB; A0A1B8SAC7; -.
DR STRING; 354243.BST28_18305; -.
DR PATRIC; fig|354243.3.peg.4546; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000092668; 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..24
FT /note="Disordered"
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; 54227 MW; 75060DD76E4087E2 CRC64;
MTEHYTTTEA GAPAPSDSDA LTVGPDGPIL LQDHYLLEQM AMFNRERTPE RQPHAKGGGA
FGRLEVTADV SAYTRAAVFA QGAETEMLAR FSTVAGERGS PDTWRDVRGF ALKFYTSEGN
FDIVGNNTPI FFFRDPMKFQ HFIRSQKRLV ASNLRDHHMQ WDFWTLSPES AHQVTYLMGD
RGLPKSWRHM NGYGSHTYSW INAAGEISWV KYHFISDQGV ENLTQQEGDR LAGADADFHQ
RDLYDAIERG EHPSWAVKVQ IMPFEEAKTY RLNPFDLTKV WPHADYPLID VGRFTLDRNV
TDYHAEIEQA AFEPSNTVPG TGLSPDKMLL ARGFSYADAH RARIGTNYNQ LPVNAPKTDV
HAYSKDGAMR FRYASDPVYA PNSVGGPAAD PARAAEVRWH ADGDMVRAAY TLREDDDDFG
QAGTLFRHVF DEEQRERLAA NIIGHVSAGV REPVLSRVFE YWRNVDEDLG RTVEAGVKAN
LS
//
