CATA_DEIRA
ID CATA_DEIRA Reviewed; 536 AA.
AC Q59337;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=katA; OrderedLocusNames=DR_1998;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RA Narumi I., Watanabe H., Hossain A., Tanaka A., Kitayama S.;
RT "Molecular cloning and nucleotide sequence of radiation-inducible catalase
RT gene from radioresistant bacterium, Deinococcus radiodurans.";
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [3]
RP DEVELOPMENTAL STAGE.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=7720013; DOI=10.1139/m95-023;
RA Wang P., Schellhorn H.E.;
RT "Induction of resistance to hydrogen peroxide and radiation in Deinococcus
RT radiodurans.";
RL Can. J. Microbiol. 41:170-176(1995).
RN [4]
RP FUNCTION, COFACTOR, SUBUNIT, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=KR1;
RX PubMed=16716939; DOI=10.1263/jbb.101.315;
RA Kobayashi I., Tamura T., Sghaier H., Narumi I., Yamaguchi S., Umeda K.,
RA Inagaki K.;
RT "Characterization of monofunctional catalase KatA from radioresistant
RT bacterium Deinococcus radiodurans.";
RL J. Biosci. Bioeng. 101:315-321(2006).
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000269|PubMed:16716939}.
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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:16716939};
CC -!- ACTIVITY REGULATION: Strongly inhibited by sodium azide and sodium
CC cyanide, and slightly inhibited by 3-amino-1,2,4-triazole.
CC {ECO:0000269|PubMed:16716939}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius. Active over a temperature
CC range from 20 to 70 degrees Celsius. Retains 100% of its initial
CC activity following incubation at 40 degrees Celsius, and 82% of its
CC activity following incubation at 50 degrees Celsius. The activity
CC decreases significantly to 30% of the initial activity following
CC incubation at 60 degrees Celsius. {ECO:0000269|PubMed:16716939};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16716939}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during stationary phase.
CC {ECO:0000269|PubMed:7720013}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; D63898; BAA09937.1; -; Genomic_DNA.
DR EMBL; AE000513; AAF11546.1; -; Genomic_DNA.
DR PIR; B75329; B75329.
DR RefSeq; NP_295721.1; NC_001263.1.
DR RefSeq; WP_010888631.1; NC_001263.1.
DR PDB; 4CAB; X-ray; 2.60 A; A/B/C/D=1-536.
DR PDBsum; 4CAB; -.
DR AlphaFoldDB; Q59337; -.
DR SMR; Q59337; -.
DR STRING; 243230.DR_1998; -.
DR EnsemblBacteria; AAF11546; AAF11546; DR_1998.
DR KEGG; dra:DR_1998; -.
DR PATRIC; fig|243230.17.peg.2221; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_0; -.
DR InParanoid; Q59337; -.
DR OMA; HVWPQKQ; -.
DR OrthoDB; 1584770at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IDA:CACAO.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; PTHR11465; 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; SSF56634; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Reference proteome.
FT CHAIN 1..536
FT /note="Catalase"
FT /id="PRO_0000085014"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 81
FT /evidence="ECO:0000250"
FT ACT_SITE 159
FT /evidence="ECO:0000250"
FT BINDING 369
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:0000250"
FT CONFLICT 152
FT /note="G -> A (in Ref. 1; BAA09937)"
FT /evidence="ECO:0000305"
FT CONFLICT 156..158
FT /note="LVG -> FVV (in Ref. 1; BAA09937)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="H -> R (in Ref. 1; BAA09937)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="Q -> K (in Ref. 1; BAA09937)"
FT /evidence="ECO:0000305"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 152..162
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:4CAB"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 240..249
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 271..281
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 287..298
FT /evidence="ECO:0007829|PDB:4CAB"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 322..331
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:4CAB"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 360..376
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:4CAB"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 456..464
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 467..481
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 486..499
FT /evidence="ECO:0007829|PDB:4CAB"
FT HELIX 501..519
FT /evidence="ECO:0007829|PDB:4CAB"
FT STRAND 529..532
FT /evidence="ECO:0007829|PDB:4CAB"
SQ SEQUENCE 536 AA; 60513 MW; 6A60CB6A8F445A59 CRC64;
MSDENNKGVG TAVQGVGGPR DGRTAPGEQG TTLTTRQGHP VHDNQNSRTV GSRGPMTLEN
YQFIEKLSHF DRERIPERVV HARGVGAHGV FRATGKVGDE PVSKYTRAKL FQEDGKETPV
FVRFSTVGHG THSPETLRDP RGFAVKFYTE DGNWDLVGNN LKIFFIRDAL KFPDLIHSQK
PSPTTNIQSQ ERIFDFFAGS PEATHMITLL YSPWGIPASY RFMQGSGVNT YKWVNDQGEG
VLVKYHWEPV QGVRNLTQMQ ADEVQATNFN HATQDLHDAI ERGDFPQWDL FVQIMEDGEH
PELDFDPLDD TKIWPREQFP WRHVGQMTLN RNPENVFAET EQAAFGTGVL VDGLDFSDDK
MLQGRTFSYS DTQRYRVGPN YLQLPINAPK KHVATNQRDG QMAYRVDTFE GQDQRVNYEP
SLLSGPKEAP RRAPEHTPRV EGNLVRAAIE RPNPFGQAGM QYRNFADWER DELVSNLSGA
LAGVDKRIQD KMLEYFTAAD ADYGQRVREG IQAKEAEMKG QKQEAPVYGT EASSLY
