ID A0A238LA73_9RHOB Unreviewed; 505 AA.
AC A0A238LA73;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132};
GN Name=katA {ECO:0000313|EMBL:SMY06315.1};
GN ORFNames=LOM8899_00438 {ECO:0000313|EMBL:SMY06315.1};
OS Flavimaricola marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Flavimaricola.
OX NCBI_TaxID=1819565 {ECO:0000313|EMBL:SMY06315.1, ECO:0000313|Proteomes:UP000201613};
RN [1] {ECO:0000313|EMBL:SMY06315.1, ECO:0000313|Proteomes:UP000201613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8899 {ECO:0000313|EMBL:SMY06315.1,
RC ECO:0000313|Proteomes:UP000201613};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|ARBA:ARBA00002974}.
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}.
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DR EMBL; FXZK01000001; SMY06315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238LA73; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000201613; 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:SMY06315.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:SMY06315.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000201613}.
FT DOMAIN 11..394
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 58
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 130
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 342
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 505 AA; 56774 MW; 0F1291451DDDFF93 CRC64;
MTDKKPGPAT TTDAGIRVQS DEHSLTVGPD GPIVLNDHYL LEQMANFNRE RIPERQPHAK
GSGAFGTFET TQDVSKYTKA KIFQPGASCD VVMRFSTVAG ERGSPDTWRD PRGFSVKMYI
EDGNFDMVGN NTPVFFIRDP MKFQHFIRSQ KRRADNNLRD HDMQWDFWTL SPESAHQVAY
LMGDRGIPRT WREMNGYSSH TYSLINAEGE KFWVKFHFHT DQGDGNAYLS QDEADKMAGM
DGDYHRRDLF NAIADGDFPS WTLKWQIMPF EDAKTYRINP FDLTKVWPHA DYPLIEVGKL
TLNRNPTDFH TEIEQAAFEP NNMVPGIGLS PDKMLLARGF SYADAHRARL GVNYKQIPVN
SAKSPVHSYS KDGAGRTEKV ADPVYAPNSY GGPSAQPEPH DEAGHWHSDG DMVRQAYTLR
EDDDDWTQAG ILVRDVMDDA ARERLVGNVV GHLTDGVSEK VLVRAFEYWR NIDSDVGDRI
EAGVREKLGG KSDAPGMASA KSISG
//
