ID   FAHD2_PONAB             Reviewed;         314 AA.
AC   Q5RCX5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Fumarylacetoacetate hydrolase domain-containing protein 2;
DE            EC=3.-.-.-;
GN   Name=FAHD2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May have hydrolase activity. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR   EMBL; CR858143; CAH90382.1; -; mRNA.
DR   RefSeq; NP_001125186.1; NM_001131714.1.
DR   AlphaFoldDB; Q5RCX5; -.
DR   SMR; Q5RCX5; -.
DR   STRING; 9601.ENSPPYP00000024293; -.
DR   GeneID; 100172076; -.
DR   KEGG; pon:100172076; -.
DR   CTD; 51011; -.
DR   eggNOG; KOG1535; Eukaryota.
DR   InParanoid; Q5RCX5; -.
DR   OrthoDB; 1216556at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.850.10; -; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; SSF56529; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Calcium; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..314
FT                   /note="Fumarylacetoacetate hydrolase domain-containing
FT                   protein 2"
FT                   /id="PRO_0000289798"
FT   BINDING         159
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P587"
FT   BINDING         161
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P587"
FT   BINDING         190
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P587"
FT   MOD_RES         203
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TC72"
FT   MOD_RES         203
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TC72"
FT   MOD_RES         234
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TC72"
SQ   SEQUENCE   314 AA;  34745 MW;  5B183CEED44E6492 CRC64;
     MLVSGRRRLL TALLQARKWP FQPSRDMRLV QFQAPHLVGP HLGLETGNGG GVINLNAFDP
     TLPKTMTQFL EQGEATLSVA RRALAAQLPV LPRSEVTFLA PVTRPDKVVC VRMNYVDHCK
     EQNVPVPKEP FIFSKFASSI VGPYDEVVLP PQSQEVDWEV ELAVVIGKKG KHIKATDAMA
     HVAGFTVAHD VSARDWQMRR NGKQWLLGKT FDTFCPLGPA LVTKDSVADP HNLKICCRVN
     GELVQSSNTN QMVFKTEDLI AWVSQFVTFY PGDVILTGTP PGVGVFRKPP VFLKKGDEVQ
     CEIEELGVII NKVV