ID A0A0J1BHF7_RHOIS Unreviewed; 493 AA.
AC A0A0J1BHF7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Catalase {ECO:0000313|EMBL:KLU05966.1};
DE EC=1.11.1.6 {ECO:0000313|EMBL:KLU05966.1};
GN ORFNames=RISK_001817 {ECO:0000313|EMBL:KLU05966.1};
OS Rhodopirellula islandica.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=595434 {ECO:0000313|EMBL:KLU05966.1, ECO:0000313|Proteomes:UP000036367};
RN [1] {ECO:0000313|EMBL:KLU05966.1, ECO:0000313|Proteomes:UP000036367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24040 / K833 {ECO:0000313|Proteomes:UP000036367};
RA Kizina J., Richter M., Glockner F.O., Harder J.;
RT "Permanent draft genome of Rhodopirellula islandicus K833.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329}.
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:KLU05966.1}.
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DR EMBL; LECT01000016; KLU05966.1; -; Genomic_DNA.
DR RefSeq; WP_047813638.1; NZ_LECT01000016.1.
DR AlphaFoldDB; A0A0J1BHF7; -.
DR STRING; 595434.RISK_001817; -.
DR PATRIC; fig|595434.4.peg.1739; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000036367; 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; cd08156; catalase_clade_3; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR040333; Catalase_3.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF9; CATALASE; 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; Heme-dependent catalase-like; 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|PIRSR:PIRSR038928-2};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038928-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KLU05966.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:KLU05966.1}.
FT DOMAIN 11..395
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 379..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 58
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 131
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 341
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:0000256|PIRSR:PIRSR038928-2"
SQ SEQUENCE 493 AA; 56488 MW; CEF2231AB2450FE2 CRC64;
MSEESKCPFQ TQQFGRVVDD NQHSQTAGPR GPVLMQDVHL VEKMAHFNRE RIPERVVHAK
GYGAFGTFTV TNDISQYCMA DLFSEVGKKT ETFARFSTVG GESGSADTAR DPRGFSLKFY
TDQGVWDLVG NNTPIFFIRD PLKFSDFIRT QKREPQNHLQ PHWRRWDFWG EVPEALHQVM
FLYSDRGTPK SARFMNGYGS HTFSMYNQDG VRHWVKFHMK TEQGSENFSA DEAIKMAGEA
PDYSTRDLFD AIERGEFPRW RMHIQVMPES DAADYKWHPF DLTKVWPHDD YPLIEVGVFE
LNRNPSNYFQ DVEQAAFEPG NLVEGIGISP DRMLQNRVLS YPDAHRYRLG VNYHQIPVNQ
PRCPYATYNR DGAMRVDGNG GGTVDYEPNK MNGPKESGRS VEPPMPVHGD GDRYDEFACD
DKDYYGQPQM FWNKVLDEGA RERLCTAISN SMADSPENIR EKMLAQFGKV HLDFEAGVRS
RLDAPKSQPI PIA
//