ID B6IP57_RHOCS Unreviewed; 529 AA.
AC B6IP57;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132};
GN Name=kat {ECO:0000313|EMBL:ACI99559.1};
GN OrderedLocusNames=RC1_2172 {ECO:0000313|EMBL:ACI99559.1};
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684 {ECO:0000313|EMBL:ACI99559.1, ECO:0000313|Proteomes:UP000001591};
RN [1] {ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI99559.1, ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT proteobacterium Rhodospirillum centenum.";
RL BMC Genomics 11:325-325(2010).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329}.
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DR EMBL; CP000613; ACI99559.1; -; Genomic_DNA.
DR RefSeq; WP_012567344.1; NC_011420.2.
DR AlphaFoldDB; B6IP57; -.
DR STRING; 414684.RC1_2172; -.
DR KEGG; rce:RC1_2172; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_5; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000001591; Chromosome.
DR GO; GO:0004096; F:catalase 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; cd08154; catalase_clade_1; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
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:SF23; CATALASE-2; 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:ACI99559.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:ACI99559.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001591}.
FT DOMAIN 9..401
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 382..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 134
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 344
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 529 AA; 60147 MW; 25341AA5AA1ABB0F CRC64;
MGSDDRTLTN RQGHPISDNQ SIRSVGERGP ATLENYQFIE KITHFDRERI PERVVHARGT
GAHGWFEAYG RIGDEPAAKY TRAKVLTRAG ERTPVFIRFS TVIGSKDSPE TARDPRGFAI
KFKTVDGVWD LVGNNLKVFF IRDAVKFPDM IHAFKPDPIS NRQEPWRFYD FVMHHPESLH
MVTWVKSPWG IPADYRHMQG SSVNTYKLVN DQGVAVLCKF SFEPKLGVRN LTAQQAAEIQ
ARDVGHATRD LHDAIERGDC PEWEMCVQIM SDDDHPELDF DPLDDTKRWP EDRFPLLPVG
RVVLDRNADN FFAEVEQASF GTGVLVDGID FSDDKMLQGR TLSYSDTQRY RVGANYLQLP
VNAPVTPART NQRDGQMAFY VDRGPENPRV NYEPSSMGGL TEAPKPERDY HQWIEGHLGR
YQTTRTADDY VQAGERYRSF EDWERDDLIA NLSDDMKQCP EHIALRMVWH FWHCAPDYGT
RVAEAAGIDL EAAKALPPLE GKPPPGQNRR GPTYTSGKLE QEPGRNAAE
//
