ID M0BZU5_9EURY Unreviewed; 753 AA.
AC M0BZU5;
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=C477_15650 {ECO:0000313|EMBL:ELZ16480.1};
OS Haloterrigena salina JCM 13891.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=1227488 {ECO:0000313|EMBL:ELZ16480.1, ECO:0000313|Proteomes:UP000011657};
RN [1] {ECO:0000313|EMBL:ELZ16480.1, ECO:0000313|Proteomes:UP000011657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13891 {ECO:0000313|EMBL:ELZ16480.1,
RC ECO:0000313|Proteomes:UP000011657};
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:ELZ16480.1}.
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DR EMBL; AOIS01000051; ELZ16480.1; -; Genomic_DNA.
DR RefSeq; WP_008895408.1; NZ_AOIS01000051.1.
DR AlphaFoldDB; M0BZU5; -.
DR STRING; 1227488.C477_15650; -.
DR PATRIC; fig|1227488.3.peg.3119; -.
DR eggNOG; arCOG00769; Archaea.
DR eggNOG; arCOG03310; Archaea.
DR OrthoDB; 53102at2157; -.
DR Proteomes; UP000011657; 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:UP000011657}.
FT DOMAIN 69..465
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 84611 MW; 1383A21C4AC08345 CRC64;
MSDDDSTPTE RDEEQPKATD GGETGESDES RSDAESGRTG TSRDDDIDEN SKQEQLDDVR
ENPEGEQLTS DHGVKISDTD NSLKAGERGP TIMEDFHFRE KMTQFDHESI PERVVHARGT
GAHGYFQPYE DPDLGEYDDL SELTKASFLQ DPDQKTPVFT RFSTVVGSRG SADTVRDVRG
FATKFYTEEG NWDLVGNNIP VFFIQDAMEF PDLVHAIKPE PDDAIPQASS AHDTFWDFAS
LKPEITHMIM WVLSGRALPR AYRMMQGFGV HTFRLVNEEG DSKFVKFHWT PKLDTSQLVW
DETQKIAGKN PDFNRQELYD AIEAGYAPEW ELGVQIFDED DAAEFDFDVL DPTKIVPETE
VPVRPIGKMV LNETPDNFFA EVEQVAFHPG NVVPGIDFSN DPLLQGRLFS YQDTQLNRFN
SANWDEIPIN RPVAERHNNQ RAGFMRQEIN EGKASYKPNS IGDDDPRETP ENEGGYEHYA
EKIEGQKIRN RSESFEDHFS QARLFWNSMT DPEKQNIVDA ARFELSKVDR MEIRERMVYD
LFNNVDHEFA KRVAEGIGVE PPEEPGDEMP THDREDSRLS IEERRDADSI ETRKIAVLVD
DGYDSDHLET VVSTLEDEGA RVKVVSKMLG DAEAENGATV EADKSHATAE SVLFDALFVP
GGEDSVDALL EQGDAKHFVA ETFKHKKPIA AAGAGTDLLE AVDLPDVEIA DDETVSSDGV
VTGGDDLEEF AEAFVDAIAE HRHWKRSPKE VPA
//
