ID L9VZB0_9EURY Unreviewed; 782 AA.
AC L9VZB0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=C495_14357 {ECO:0000313|EMBL:ELY42505.1};
OS Natronorubrum sulfidifaciens JCM 14089.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1230460 {ECO:0000313|EMBL:ELY42505.1, ECO:0000313|Proteomes:UP000011661};
RN [1] {ECO:0000313|EMBL:ELY42505.1, ECO:0000313|Proteomes:UP000011661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14089 {ECO:0000313|EMBL:ELY42505.1,
RC ECO:0000313|Proteomes:UP000011661};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
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:ELY42505.1}.
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DR EMBL; AOHX01000045; ELY42505.1; -; Genomic_DNA.
DR RefSeq; WP_008164068.1; NZ_AOHX01000045.1.
DR AlphaFoldDB; L9VZB0; -.
DR STRING; 1230460.C495_14357; -.
DR PATRIC; fig|1230460.4.peg.2922; -.
DR eggNOG; arCOG00769; Archaea.
DR eggNOG; arCOG03310; Archaea.
DR OrthoDB; 53102at2157; -.
DR Proteomes; UP000011661; Unassembled WGS sequence.
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:UP000011661}.
FT DOMAIN 96..493
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 87368 MW; 62C6B4D515292FB0 CRC64;
MVANDSNTDD RNDEQPKSTD NNANQPDARD DQPEREAIAD DPERQERADG GDGGGSRSDS
ESQAGTSDDQ EGESAENSKQ AQLDEVRENS EGEKLTTDHG VKVSDTDNSL KAGERGPTIM
EDFHFREKMT QFDHESIPER VVHARGTGAH GYFQPYEDPD LGDEYDDIEE LTKAKVLTNP
DQKTPVFVRF STVVGSRGSS DTVRDVRGFA TKFYTKEGNW DLVGNNMPPF FIQDAMEFPD
LVHAIKPEPD DGMPQASAAH DTFWDFASLK PETTHMLMWV LSGRALPRAY RMMQGFGVHT
FRLVNDDGES VFVKFHWTPE LGTHQLVWDE TTKLWGKDSD FNRKGLYDVI EEGYDPEWEL
GVQIFDEEQA EAFDFDVLDP TKIVPETEVP VRPIGKMVLN ETPDNFFAET EQVAFHPGNV
VPGIDFSNDP LLQGRLFSYQ DTQLNRFGSA NWDEIPINRP IAERHNNQRA GFMRQEINEG
TASYKPNSIG DDDPQEVPEE EGGYEHFAEK ISGEKIRNRS DSFEDHFTQA RLFWNSMSEP
EQQNIVDAAH FELGKVDRME IRERMVYDLF NNVDHEFAKR VAEGIGVDPP DEPGEEMPTH
DREDPSLSME NRTPDTIETR KIAMLIDDGF DDEHVSTLRS ALEEDGARVK VVSKVLGEKS
GADGGTVDPD KHHVAAASVS FDAIVVPGGS ESVDALCQQG DPKQFVAEAF KHYKPIAAVG
EGTELFEAVD LPDTEIADEG DLESDAGVVT CRNDDLEAFA AAFIDAIAEH RHWGRSPEGV
PA
//
