CATE_RHIME
ID CATE_RHIME Reviewed; 705 AA.
AC Q9X576;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Catalase C;
DE EC=1.11.1.6;
DE AltName: Full=KAT2;
GN Name=katE; Synonyms=catC, katC; OrderedLocusNames=RB0010;
GN ORFNames=SMb20007;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RCR2011 / SU47;
RX PubMed=10198032; DOI=10.1128/jb.181.8.2634-2639.1999;
RA Sigaud S., Becquet V., Frendo P., Puppo A., Herouart D.;
RT "Differential regulation of two divergent Sinorhizobium meliloti genes for
RT HPII-like catalases during free-living growth and protective role of both
RT catalases during symbiosis.";
RL J. Bacteriol. 181:2634-2639(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide. Could
CC protect cells in nodules which have a high potential to produce
CC hydrogen peroxide because of the strong reducing conditions required
CC for nitrogen fixation and the action of several proteins.
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:0000255|PROSITE-ProRule:PRU10013};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- INDUCTION: A threefold increase of the activity arises after exposure
CC to heat stress (37 degrees Celsius), to sodium chloride or ethanol for
CC one hour. Not inducible by hydrogen peroxide.
CC -!- MISCELLANEOUS: Either KatA or KatC is absolutely required for the
CC protection of the nitrogen fixation process.
CC -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC {ECO:0000305}.
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DR EMBL; AF121348; AAD21077.1; -; Genomic_DNA.
DR EMBL; AL591985; CAC48410.1; -; Genomic_DNA.
DR PIR; B95843; B95843.
DR RefSeq; NP_436550.1; NC_003078.1.
DR RefSeq; WP_010974935.1; NC_003078.1.
DR AlphaFoldDB; Q9X576; -.
DR SMR; Q9X576; -.
DR STRING; 266834.SM_b20007; -.
DR PeroxiBase; 6330; SmeKat02.
DR EnsemblBacteria; CAC48410; CAC48410; SM_b20007.
DR GeneID; 61600033; -.
DR KEGG; sme:SM_b20007; -.
DR PATRIC; fig|266834.11.peg.4913; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_3_0_5; -.
DR OMA; VMWQMSD; -.
DR Proteomes; UP000001976; Plasmid pSymB.
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 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; PTHR42821; 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; SSF52317; 1.
DR SUPFAM; SSF56634; SSF56634; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 2: Evidence at transcript level;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Plasmid; Reference proteome.
FT CHAIN 1..705
FT /note="Catalase C"
FT /id="PRO_0000084974"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 375
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 113
FT /note="F -> C (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="R -> H (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="D -> H (in Ref. 1; AAD21077)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="D -> H (in Ref. 1; AAD21077)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="A -> G (in Ref. 1; AAD21077)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="V -> L (in Ref. 1; AAD21077)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="A -> R (in Ref. 1; AAD21077)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="I -> V (in Ref. 1; AAD21077)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="G -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 430..447
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="A -> G (in Ref. 1; AAD21077)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="K -> N (in Ref. 1; AAD21077)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="T -> A (in Ref. 1; AAD21077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 705 AA; 78628 MW; CC856B24B70FE5ED CRC64;
MAKKPSAPNN TKPATIHDQK ATRGNGGELH QIAEGDTPVL TTAQGGPVAD DQNSLRAGER
GPTLIEDFHF REKIFHFDHE RIPERVVHAR GYGVHGFFET YESLAAYTRA DLFQRPGERT
PAFVRFSTVA GSKGSFDLAR DVRGFAVKIY TKEGNWDLVG NNIPVFFIQD AIKFPDVIHS
VKPEPDREFP QAQSAHDNFW DFISLTPESM HMIMWVMSDR AIPRSFRFME GFGVHTFRFV
NAKDESTFVK FHWKPKLGLQ SVVWNEAVKI NGADPDFHRR DMWQAIQSGN FPEWDLHVQL
FDQDFADKFD FDILDPTKII PEEVLPTKPV GRLVLDRMPE NFFAETEQVA FMTQNVPPGI
DFSDDPLLQG RNFSYLDTQL KRLGSPNFTH LPINAPKCPF QHFQQDGHMA MRNPVGRVNY
QPNSWGEGPR ESPMKGFRHF PSEEQGPKLR IRAESFADHY SQARQFFISQ TPPEQRHIAD
ALTFELSKVE TPVIRERMVA HLLNIDETLG KKVGHALGLE TMPKPADAAV ATRQDLDPSP
ALSIIQRGPK RFEGRKLGIL ATDGADGALL DALIAAVEKE KAAFELIAPK VGGFTASDGK
RIAAHQMLDG GPSVLYDAVV LLPSAEAVTD LIDVATARDF VADAFAHCKY IGYAGAAVPL
LERAGIAELL DEGTIELTDA ASAAAFLTEI GKLRVWGREP SVKLK
