ID L0K5I0_9EURY Unreviewed; 750 AA.
AC L0K5I0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|RuleBase:RU000498};
GN ORFNames=Natoc_3642 {ECO:0000313|EMBL:AGB39358.1};
OS Natronococcus occultus SP4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronococcus.
OX NCBI_TaxID=694430 {ECO:0000313|EMBL:AGB39358.1, ECO:0000313|Proteomes:UP000010878};
RN [1] {ECO:0000313|EMBL:AGB39358.1, ECO:0000313|Proteomes:UP000010878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP4 {ECO:0000313|EMBL:AGB39358.1,
RC ECO:0000313|Proteomes:UP000010878};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., Klenk H.-P.,
RA Klenk H.-P.;
RT "FINISHED of Natronococcus occultus SP4, DSM 3396.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC Evidence={ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|RuleBase:RU000498}.
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DR EMBL; CP003929; AGB39358.1; -; Genomic_DNA.
DR RefSeq; WP_015322792.1; NC_019974.1.
DR AlphaFoldDB; L0K5I0; -.
DR STRING; 694430.Natoc_3642; -.
DR GeneID; 14402409; -.
DR KEGG; nou:Natoc_3642; -.
DR eggNOG; arCOG00769; Archaea.
DR eggNOG; arCOG03310; Archaea.
DR HOGENOM; CLU_010645_3_0_2; -.
DR OrthoDB; 53102at2157; -.
DR Proteomes; UP000010878; 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; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 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|RuleBase:RU000498};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|RuleBase:RU000498};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000498};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000498};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000498};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498};
KW Reference proteome {ECO:0000313|Proteomes:UP000010878}.
FT DOMAIN 65..461
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 84080 MW; 5AD00C01752DD579 CRC64;
MTADNSSDER EPETTGGERE PRTDGSGTDP GSTGTSDDAG GEIDENSKHE QLEEVRENSD
GEHLTTDHGV KVSDTDNSLK AGERGPTIME DFHFREKMTQ FDHESIPERV VHARGTGAHG
YFQPYEDPDL GEYDDISELT KASLFQDPDK KTPVFTRFST VVGSRGSSDT VRDVRGFATK
FYTEDGNWDL VGNNMPPFFI QDAMEFPDLV HAIKPEPDDG IPQASAAHDT FWDFASLKPE
ITHMIMWVLS GRALPRAYRM MQGFGVHTFR LVNDDGESVF VKFHWTPKLG THQLVWDETT
KLWGKSSDFN RKGLYDVIEE GYDPEWELGV QIFDEEQAAE FDFDVLDPTK IVPETEVPVR
PIGKMVLNET PDNFFAEVEQ VAFHPGNVVP GIDFSNDPLL QGRLFSYQDT QLNRFGGANW
DEIPINRPIA ERHNNQRAGF MRQEINEGKV SYKPNSIGDD DPQEAPAEEG GYEHYAEKVD
GQKIRNRSDS FENHFTQARL FWNSMSEPEK QNIVDAAHFE LGKVERVEIR ERMVYDLFNN
VDHEFAKRVA EGIGVEPPEE PGDEMPTHDR EDPSLSMENR TPDTIETRKI AMLIDDGFDD
EHVSKLRSAL EEEGARVKII SKVLGEKSGV DGETVEPDKH HVAAASVSFD AVVIPGGDES
VDAMRGQGDP KHFVAEAFKH YKPIAAVGEG TELFEAVDLP DTEIADEGDL VSDAGVVTCR
SDDLESFAEA FVDAIAQHRH WDRDPEEVPA
//
