ID Q0SJL1_RHOJR Unreviewed; 485 AA.
AC Q0SJL1;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Catalase {ECO:0000313|EMBL:ABG92275.1};
DE EC=1.11.1.6 {ECO:0000313|EMBL:ABG92275.1};
GN Name=katA {ECO:0000313|EMBL:ABG92275.1};
GN OrderedLocusNames=RHA1_ro00439 {ECO:0000313|EMBL:ABG92275.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG92275.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG92275.1; -; Genomic_DNA.
DR RefSeq; WP_011593712.1; NC_008268.1.
DR AlphaFoldDB; Q0SJL1; -.
DR KEGG; rha:RHA1_ro00439; -.
DR PATRIC; fig|101510.16.peg.467; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_4_1_11; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000008710; 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:SF61; 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:ABG92275.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:ABG92275.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 8..394
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 55
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 128
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 338
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 485 AA; 54293 MW; 33167B89A4F9AFBC CRC64;
MTNPNGLTTV AGAPVPDNQN SLTAGARGPM LLQDVWLLEK LAHFDREVIP ERRMHAKGSA
AFGTFRVTHD ITAHTNAAVF SEIGKRTEVF LRFSTVAGER GAADAERDIR GFAVRFYTEQ
GNWDVVGNNT PVFFFRDPLK FPDLNHAVKR DPRTNLRSAE NNWDFWTNLP EALHQITIVM
SDRGIPNGYR HMHGFGSHTF SFVNDAGERS WVKFHFRTQQ GIKNLTDEEA AAVVAGDRES
AQRDLFNAIE EGNYPKWTLF VQIMPEADAQ TYHYHPFDLT KVWSKKDYPL IEVGELELDR
NPENYHADVE QAAFSPANIV PGIGFSPDRM LQGRLFSYGD AARYRLGVNH HQIPVNSPRG
ATHVNSFHRD GVMRVDGNQG SVPSIEPNSH GRFADQRSYA EPPLEVGVVA DRFDYRADDD
NYFEQPGNLF RSMSAEQQTL LFENTARAIT GASAAVIERH IVNCAQADPA YGEGVRKACE
AFGAL
//
