ID A9WQD9_RENSM Unreviewed; 677 AA.
AC A9WQD9;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN OrderedLocusNames=RSal33209_0845 {ECO:0000313|EMBL:ABY22589.1};
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Renibacterium.
OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY22589.1, ECO:0000313|Proteomes:UP000002007};
RN [1] {ECO:0000313|Proteomes:UP000002007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC {ECO:0000313|Proteomes:UP000002007};
RX PubMed=18723615; DOI=10.1128/JB.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
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|ARBA:ARBA00000720,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR602481-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR602481-1};
CC -!- SIMILARITY: Belongs to the Fur family. {ECO:0000256|ARBA:ARBA00007957}.
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|RuleBase:RU000498}.
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DR EMBL; CP000910; ABY22589.1; -; Genomic_DNA.
DR AlphaFoldDB; A9WQD9; -.
DR SMR; A9WQD9; -.
DR STRING; 288705.RSal33209_0845; -.
DR KEGG; rsa:RSal33209_0845; -.
DR eggNOG; COG0735; Bacteria.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_4_1_11; -.
DR Proteomes; UP000002007; Chromosome.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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 CDD; cd07153; Fur_like; 1.
DR Gene3D; 3.30.1490.190; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR040333; Catalase_3.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR002481; FUR.
DR InterPro; IPR043135; Fur_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF9; CATALASE; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF01475; FUR; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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|PIRSR:PIRSR602481-1};
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:UP000002007};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR602481-1}.
FT DOMAIN 180..563
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR602481-1"
SQ SEQUENCE 677 AA; 74706 MW; 3D8E4276BFF17F0F CRC64;
MTGVMTVTRD TVASSSDWEQ TQQDWETSLR AHGRRVTKQR LAVLAAAHMA PHQDAEHIWR
EACTELPELT LQSVYTVLAD LTGLGLLRKI EPTSGPARYE TRVGDNHHHA VCSVCGRIED
IDCAVGHAPC LEPTSSSMAI YRAEVTFHGI CADCASLEST DFTPPQRTTT HRRVMTVNST
TQSGAPVQSD AHSQSVGQDG AIALTDHYLV EKLAQFNRER VPERVVHAKG GGAFGTFVTK
EDVSKYTKAA LFQPGAETEM LIRFSSVAGE QGSPDTWRDP RGFAIKFYTS EGNYDLVGNN
TPVFFIRDGI KFPDFIHSQK RLPGSNLRDA DMQWDFWTLS PESAHQVTWL MGDRGLPLSW
RKMQGYSSHT YQWINAEGER FWVKYHFHTN QGVEGMSNEQ AAELAGSDGD HHIRDLYESI
DTGDFPSWEL HVQVMPYEDA KDYRFNPFDL TKVWPKADYP LIHVGTMTLN KNPENYFAQI
EQATFAPSNF VPGIAASPDK MLQARIFSYA DAHRYRVGTN HAQIPVNAPK NEVHNYSQNG
AGRYTFNSAA TPNYAPNSKN GAAADETQFQ AGGWENDGAL TIAAARLHSE DSDFGQAGTL
YREVYDDGAK ARFLETITGA VGGVQDADIK ERAIQYWTNV DSDLGAKLRA NLGAGDKGSA
DGAVQQGGLT GEHDGAQ
//
