ID A0A0C2GTD4_9BILA Unreviewed; 434 AA.
AC A0A0C2GTD4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Catalase {ECO:0000313|EMBL:KIH60396.1};
GN ORFNames=ANCDUO_09357 {ECO:0000313|EMBL:KIH60396.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH60396.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH60396.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH60396.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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; KN731000; KIH60396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2GTD4; -.
DR SMR; A0A0C2GTD4; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
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 Gene3D; 2.40.180.10; Catalase core domain; 2.
DR InterPro; IPR018028; Catalase.
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; 2.
DR Pfam; PF06628; Catalase-rel; 1.
DR PIRSF; PIRSF038928; Catalase_clade1-3; 2.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 2.
DR PROSITE; PS00437; CATALASE_1; 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 Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000054047}.
FT DOMAIN 1..275
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT BINDING 221
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 434 AA; 50444 MW; 9BCFCB3894EBFEA2 CRC64;
MVVQFSSFKV GNNTPIFFIR DPIQFPNFIH TQKRNPQTHL KDPNMVWDFW GLRPESTHQV
MFLMSDRGTP DGFRHMNGYG SHTFKLVNAE GTPVYCKFHW KPQKIKNLMA DEAARLCGED
PDYAIRDLYN AIERGDYPTW NFFIQVMTFE QAEKWPMNPF DVTKVWPHGE FPLIPVGKMV
LNRNPKNYFA EVEQSAFSPA HVVPGVEFSP DKMLQGRLFS YTDTHFHRLG TNYLHLPINC
PYRARAHNTQ RDGPACFDNQ GDAPNYFPNS FNGHVECPRS AESKYTVTGD VARHESANDD
NFEQPRVFWQ KILNEDERTR LVENIFNAMK DCKPFIQDRA IQNFGKVDAE FGNRLRKNID
TYISQKTEIS SPGAHGYFEV THDITKYCKA DLFNKVGKQT PVFARFSTVG KFEQDFSFFR
KEFIATNHNR NLVQ
//
