CATA_RHIME
ID CATA_RHIME Reviewed; 494 AA.
AC P95631;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Catalase A;
DE EC=1.11.1.6;
GN Name=katA; OrderedLocusNames=R00764; ORFNames=SMc00819;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
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=8955300; DOI=10.1128/jb.178.23.6802-6809.1996;
RA Herouart D., Sigaud S., Moreau S., Frendo P., Touati D., Puppo A.;
RT "Cloning and characterization of the katA gene of Rhizobium meliloti
RT encoding a hydrogen peroxide-inducible catalase.";
RL J. Bacteriol. 178:6802-6809(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(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.
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 -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; U59271; AAC44649.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45336.1; -; Genomic_DNA.
DR RefSeq; NP_384870.1; NC_003047.1.
DR RefSeq; WP_010968798.1; NC_003047.1.
DR AlphaFoldDB; P95631; -.
DR SMR; P95631; -.
DR STRING; 266834.SMc00819; -.
DR PeroxiBase; 4297; SmeKat01.
DR EnsemblBacteria; CAC45336; CAC45336; SMc00819.
DR GeneID; 61602233; -.
DR KEGG; sme:SMc00819; -.
DR PATRIC; fig|266834.11.peg.2148; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_5; -.
DR OMA; WTCYVQV; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; cd08156; catalase_clade_3; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR040333; Catalase_3.
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 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Periplasm;
KW Peroxidase; Reference proteome.
FT CHAIN 1..494
FT /note="Catalase A"
FT /id="PRO_0000084996"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 55
FT /evidence="ECO:0000250"
FT ACT_SITE 127
FT /evidence="ECO:0000250"
FT BINDING 337
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 1..19
FT /note="MTDRPTITTTAGAPVPDNQ -> MPPPLPERRHLICACVGTYCGCGSNPPSG
FT SSPFVPASFFVPAEGTAEPRCGGVSSPRSRAGFSPRIRALISSPVSVSYSSKPSARAT
FT (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 56009 MW; 39FA86606D2D83D7 CRC64;
MTDRPTITTT AGAPVPDNQN SLTAGPRGGI MLQDYQLIEK LAHQNRERIP ERVVHAKGWG
AFGSLKITGD ISQYTRAKCL QPGAETPMLA RFSTVAGEQG AADHERDVRG FALKFYTDEG
NWDLVGNNTP VFFIRDPYKF PDFIHTQKRH PKTNLRSATA MWDYWSLSPE SLHQVTILMS
DRGLPQTPMH MNGYGSHTYS FWNDAGERYW VKFHFKTQQG HKFFTNEEGE AVIGKTREGY
QESLFYAIEN GEFPRWTVQV QIMPELDVEK TPYNPFDLTK VWPHADYPPV EIGVLELNRN
PENYFAEIEN AAFSPSNIVP GIGFSPDKVL QARIFSYADA HRYRLGTHYE HIPVNQPRCP
VHHYHRDGQM NTYGGIRTGN PDAYYEPNSF NGPAEQPLAK EPPLRIDGDM SRYDHRVGND
DYVQVRALFG LFDEGQKSRL FSNIAAAMGG VPGEIIERQL IHFARVHPEY EAGVRQALKT
AHGYEADTIS TAAE
