ID A0A2T1LV83_9CHRO Unreviewed; 714 AA.
AC A0A2T1LV83;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 Name=katE {ECO:0000313|EMBL:PSF35583.1};
GN ORFNames=C7H19_16395 {ECO:0000313|EMBL:PSF35583.1};
OS Aphanothece hegewaldii CCALA 016.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Aphanothece.
OX NCBI_TaxID=2107694 {ECO:0000313|EMBL:PSF35583.1, ECO:0000313|Proteomes:UP000239001};
RN [1] {ECO:0000313|EMBL:PSF35583.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF35583.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSF35583.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF35583.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:PSF35583.1}.
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DR EMBL; PXOH01000019; PSF35583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1LV83; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000239001; Unassembled WGS sequence.
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:UP000239001}.
FT DOMAIN 30..417
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 77
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 150
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 74
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 114
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 163
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 360
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 364
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 371
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 714 AA; 80299 MW; 1E6A05964242E055 CRC64;
MSEPNNHQIN EDSKIKDMEP FRQEVGEYMT TNQGVGVSDT DNSLKAGERG PSLLEDFHHL
EKMSHFDRER IPERVVHARG AGAHGYFQVY ESMAKYTKAK FLQDPSVKTP VFVRFSNVGG
SRGSADTVRD VRGFSIKFYT EEGNYDFVGN NIPVFFIQDG IKFPDIIHAV KPEPNNEIPQ
ASSAHDNFWD FISLVPESMH MIMWFLSDRT LAKSYRMIQG FGVHTFRFVN EEGKARFVKL
HWKPLLGVHS FVFDEAQKLS GKDPDYHRRD LWEMIEMGHY PEYELGVQII EEEDENKFGF
DILDSTKFIP EELVPVIPVG KMVLNRNPDN YFAETEQSAF HPGRVVPGID FTDDPLLQSR
VFSYHDTQLY RLGANFAHLP INRPVCPVHN NQQDGFMQTN IKQGRTNYYP NSLGGGCPMM
TPEGMSAFSH YSESVQGNKV RKRAESFKKD YFSQATLFWN SLTDIEKDHL VKAAHFELGK
VQTKAIRERM VELFNQVDHE LAKLVAKGIG VAAPTKAVTE NHGQSSPAVS MEKMKEKMEK
SAKTRQVAIL AADGVNSSQV MEIKEILKQA GVLPQVVSEF KGTIKGADGQ EIEVNQTFLT
AASVMFDAVY VPGGKQSVEM LVNKDDAIEF VHEAFKHCKP IAATGEGVEL LKGAHLKGVN
FDQAGSNGKA KADQGIVTSQ DGSDMQSIGQ KFIEAIAKGR FWTREQMEKK MVPA
//
