ID A3UA09_CROAH Unreviewed; 713 AA.
AC A3UA09;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN OrderedLocusNames=CA2559_11433 {ECO:0000313|EMBL:EAP86645.1};
OS Croceibacter atlanticus (strain ATCC BAA-628 / HTCC2559 / KCTC 12090).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Croceibacter.
OX NCBI_TaxID=216432 {ECO:0000313|EMBL:EAP86645.1, ECO:0000313|Proteomes:UP000002297};
RN [1] {ECO:0000313|EMBL:EAP86645.1, ECO:0000313|Proteomes:UP000002297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-628 / HTCC2559 / KCTC 12090
RC {ECO:0000313|Proteomes:UP000002297};
RX PubMed=20639333; DOI=10.1128/JB.00733-10;
RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT "The complete genome sequence of Croceibacter atlanticus HTCC2559T.";
RL J. Bacteriol. 192:4796-4797(2010).
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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|PIRNR:PIRNR038927,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC {ECO:0000256|ARBA:ARBA00010660}.
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DR EMBL; CP002046; EAP86645.1; -; Genomic_DNA.
DR RefSeq; WP_013188026.1; NC_014230.1.
DR AlphaFoldDB; A3UA09; -.
DR STRING; 216432.CA2559_11433; -.
DR PeroxiBase; 7265; CatKat01.
DR KEGG; cat:CA2559_11433; -.
DR eggNOG; COG0693; Bacteria.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_3_0_10; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000002297; Chromosome.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 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 Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW Reference proteome {ECO:0000313|Proteomes:UP000002297}.
FT DOMAIN 31..419
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 78
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 151
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 75
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 115
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 164
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 361
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 365
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:PIRSR038927-2"
FT BINDING 372
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 713 AA; 80481 MW; B4A89367C3778A45 CRC64;
MSDKENLQPD SNSKTDQLSS YTKDSEGKNL TTNQGLKVND TNNSLKAGER GSTLLEDFLL
REKITSFDHE RIPERIVHAR GSAAHGHFEL YKSIEKYTKA GLFTDTSKKT PVFVRFSTVA
GSKGSPDLAR DVRGFAVKFY TEEGTWDLVG NNMPIFFIQD AMKFPDLIHS VKPEPNNEIP
QAASAHDTFY DFVSHAPETL HNHIWAMSDR AIPRSYRMME GFGIHTFRFI NKEGKSHFVK
FHWKPVLGVH SVTWEEAVKI NGVDADFHRR DLWEAIEAGQ YPEWEFGIQV VPEEDEHKYD
FDLLDPTKLI PEDMVPVEIV GKMTLNRNPS NFFAETEQVA FLPGHIIPGL DFTNDPLLQG
RLFSYRDTQL SRLGSPNFHQ IPINRPVTPA HNNQRDGHMQ TEIPKGQTAY FPNTLGGGCP
HLAKMAEGGF TSYEERIDAK KVRTRSESFS DHFSQPALFY RSLEEWEKKH VANAYSFELG
KCNQKHIKER MLWLINQIDE DLANTVSENL GLSIPDDIEQ PINQSIGADA DVEKFQPSAK
KVYLEKDKSL SQAHTKFDSI ATRQIAVLAA NGFSMDDFKT FTDALEDEGA VCKIIAPHGG
TIKCDQDMDH EVDAAISTTE SVLFDAIFVP GGKDSVDKLL KTGKYSKFIS EAFKHCKAIA
VCNEGEELLK NSYIKSYDDD KAVFVNGKPK NFIDAIAQHR NWDRMEAASD IPV
//
