ID A0A091TEG0_PHALP Unreviewed; 507 AA.
AC A0A091TEG0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
DE Flags: Fragment;
GN ORFNames=N335_13574 {ECO:0000313|EMBL:KFQ72844.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ72844.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ72844.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ72844.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|RuleBase:RU004142}.
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|ARBA:ARBA00000720,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000256|ARBA:ARBA00001937};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR EMBL; KK449746; KFQ72844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091TEG0; -.
DR PhylomeDB; A0A091TEG0; -.
DR Proteomes; UP000053638; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; IPR002226; Catalase_haem_BS.
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; 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|PIRSR:PIRSR038928-2};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|RuleBase:RU000498};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038928-2}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000498};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498};
KW Reference proteome {ECO:0000313|Proteomes:UP000053638}.
FT DOMAIN 7..392
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 54
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 127
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 337
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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ72844.1"
FT NON_TER 507
FT /evidence="ECO:0000313|EMBL:KFQ72844.1"
SQ SEQUENCE 507 AA; 57525 MW; 3E71280BAE52D1D3 CRC64;
QKADVLTTGA GNPVGDKLNI LTVGPHGPLL VQDVVFTDEM AHFDRERIPE RVVHAKGAGA
FGYFEVTHDI TKYCKAKVFE HIGKRTPIAI RFSTVAGESG SADTVRDPRG FAMKFYTEEG
NWDLVGNNTP IFFIRDAMLF PSFIHSQKRN PQTHLKDPDM VWDFWSLRPE SLHQVSFLFS
DRGIPDGYRH MNGYGSHTFK LVNASGKAVY CKFHVKTDQG IKNLSVEEAG RLASTDPDYG
IRDLYNAIAK GDYPSWSFYI QVMTFEEAEK FPFNPFDLTK IWPHGDYPLI PVGKLVLNRN
PVNYFAEVEQ MAYDPSNMPP GIEPSPDKML QGRLFSYPDT HRHRLGPNYL QIPVNCPFRT
RVANYQRDGP MCVSDNQGGA PNYYPNSFTG PEDQPVVKES RVSVSGDVQR FNSANEDNVT
QVREFYTKVL KEDERQRLCK NIADHLKDAQ LFIQKRAVKN FTDVHPDYGA RIQALLDKYN
ADSGKKDVIR TYTQSTSRVS AKERSNL
//
