ID A0A0B1SVW8_OESDE Unreviewed; 306 AA.
AC A0A0B1SVW8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Fumarylacetoacetase {ECO:0000256|ARBA:ARBA00014741, ECO:0000256|RuleBase:RU366008};
DE EC=3.7.1.2 {ECO:0000256|RuleBase:RU366008};
DE AltName: Full=Fumarylacetoacetate hydrolase {ECO:0000256|RuleBase:RU366008};
GN ORFNames=OESDEN_10709 {ECO:0000313|EMBL:KHJ89463.1};
OS Oesophagostomum dentatum (Nodular worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Oesophagostomum.
OX NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ89463.1, ECO:0000313|Proteomes:UP000053660};
RN [1] {ECO:0000313|EMBL:KHJ89463.1, ECO:0000313|Proteomes:UP000053660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ89463.1,
RC ECO:0000313|Proteomes:UP000053660};
RA Mitreva M.;
RT "Draft genome of the hookworm Oesophagostomum dentatum.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H(+);
CC Xref=Rhea:RHEA:10244, ChEBI:CHEBI:13705, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18034, ChEBI:CHEBI:29806; EC=3.7.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000353,
CC ECO:0000256|RuleBase:RU366008};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU366008};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU366008};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 6/6.
CC {ECO:0000256|RuleBase:RU366008}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000256|ARBA:ARBA00010211,
CC ECO:0000256|RuleBase:RU366008}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN554186; KHJ89463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1SVW8; -.
DR UniPathway; UPA00139; UER00341.
DR Proteomes; UP000053660; Unassembled WGS sequence.
DR GO; GO:0004334; F:fumarylacetoacetase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR InterPro; IPR005959; Fumarylacetoacetase.
DR InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR InterPro; IPR036462; Fumarylacetoacetase_N_sf.
DR NCBIfam; TIGR01266; fum_ac_acetase; 1.
DR PANTHER; PTHR43069; FUMARYLACETOACETASE; 1.
DR PANTHER; PTHR43069:SF2; FUMARYLACETOACETASE; 1.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR SUPFAM; SSF56529; FAH; 1.
DR SUPFAM; SSF63433; Fumarylacetoacetate hydrolase, FAH, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU366008};
KW Hydrolase {ECO:0000256|RuleBase:RU366008};
KW Magnesium {ECO:0000256|RuleBase:RU366008};
KW Metal-binding {ECO:0000256|RuleBase:RU366008};
KW Phenylalanine catabolism {ECO:0000256|RuleBase:RU366008};
KW Reference proteome {ECO:0000313|Proteomes:UP000053660};
KW Tyrosine catabolism {ECO:0000256|RuleBase:RU366008}.
FT DOMAIN 46..302
FT /note="Fumarylacetoacetase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01557"
SQ SEQUENCE 306 AA; 33662 MW; 7D37AE45B1BDB407 CRC64;
MKSFVPVPEG SDFPIQNCPY GVFSTKDNVS RFYKIFFDSQ YLWKWLPVGY HGRASSVIPS
GTPARSPRGQ LKLEGATEPT YGASRLLDFE LEMAFFVGGP ATELGQPISI EKTEDHIFGM
VLMNDWSARD IQAWEYVPLG PFLGKSFGTT ISPWVVSMEA LRPFMVANPE QDPAPLSYLA
HSDPYTLDIN LGVTIKPEGG EDHSVCKTSF KHLYWTLKQQ LAHHTVNGCN VNPGDLMGSG
TVSGPEEGAY GSMLELSWRG AKTVPVGDQT RKFLQDGDEV NLVGFCEKDG VRIGFGECRG
KVLPAL
//
