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FAAA_DICDI
ID   FAAA_DICDI              Reviewed;         427 AA.
AC   Q1ZXQ1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Fumarylacetoacetase;
DE            Short=FAA;
DE            EC=3.7.1.2 {ECO:0000250|UniProtKB:P35505};
DE   AltName: Full=Beta-diketonase;
DE   AltName: Full=Fumarylacetoacetate hydrolase;
GN   Name=fah; ORFNames=DDB_G0271094;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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:0000250|UniProtKB:P35505};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P35505};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P35505};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 6/6.
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR   EMBL; AAFI02000005; EAS66937.1; -; Genomic_DNA.
DR   RefSeq; XP_001134473.1; XM_001134473.1.
DR   AlphaFoldDB; Q1ZXQ1; -.
DR   SMR; Q1ZXQ1; -.
DR   STRING; 44689.DDB0231609; -.
DR   PaxDb; Q1ZXQ1; -.
DR   PRIDE; Q1ZXQ1; -.
DR   EnsemblProtists; EAS66937; EAS66937; DDB_G0271094.
DR   GeneID; 8617161; -.
DR   KEGG; ddi:DDB_G0271094; -.
DR   dictyBase; DDB_G0271094; fah.
DR   eggNOG; KOG2843; Eukaryota.
DR   HOGENOM; CLU_026207_2_0_1; -.
DR   InParanoid; Q1ZXQ1; -.
DR   OMA; YWTAAQQ; -.
DR   PhylomeDB; Q1ZXQ1; -.
DR   Reactome; R-DDI-8963684; Tyrosine catabolism.
DR   UniPathway; UPA00139; UER00341.
DR   PRO; PR:Q1ZXQ1; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0004334; F:fumarylacetoacetase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1902000; P:homogentisate catabolic process; IBA:GO_Central.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR   GO; GO:0006572; P:tyrosine catabolic process; IBA:GO_Central.
DR   Gene3D; 2.30.30.230; -; 1.
DR   Gene3D; 3.90.850.10; -; 1.
DR   InterPro; IPR005959; Fumarylacetoacetase.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   InterPro; IPR015377; Fumarylacetoacetase_N.
DR   InterPro; IPR036462; Fumarylacetoacetase_N_sf.
DR   PANTHER; PTHR43069; PTHR43069; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   Pfam; PF09298; FAA_hydrolase_N; 1.
DR   SUPFAM; SSF56529; SSF56529; 1.
DR   SUPFAM; SSF63433; SSF63433; 1.
DR   TIGRFAMs; TIGR01266; fum_ac_acetase; 1.
PE   3: Inferred from homology;
KW   Calcium; Hydrolase; Magnesium; Metal-binding; Phenylalanine catabolism;
KW   Reference proteome; Tyrosine catabolism.
FT   CHAIN           1..427
FT                   /note="Fumarylacetoacetase"
FT                   /id="PRO_0000318805"
FT   ACT_SITE        137
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         130
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         204
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         206
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         239
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         239
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         259
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         263
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
SQ   SEQUENCE   427 AA;  47429 MW;  7A83720EFB17516A CRC64;
     MSILKSFIEV SEDSHFPIQN LPYGVFKPTL NDQARIGVAI GDFVCDLSVL ADLKLFDGKL
     KDTKVFHQEN LNSFMSLGKE LWSEARKTIQ NLLSSETSTI RDNKEYREKI FHSISSVTML
     LPARIGDYTD FYASKEHATN VGIMFRGKEN ALMPNWVHLP VGYHGRSSSI VVSGTPLKRP
     WGQTKSDEPD SLPTFNPCRL LDFELEMGAL IGGESTKLGE PISIESAKDH IFGLVLLNDW
     SARDIQKWEY VPLGPFLAKN FGSTISPWVV TMEALQPFAT KPPTQDPQPM KYLQEQGNTT
     FDIELSVSIK SPKMSKPHKV STSNLKYMYW TLTQQLAHHT VNGCNMNAGD LLGTGTISGP
     TEDSYGSMLE LSWKGSKVVS LGTETNEERK FIQDGDSVIL SGLCKGNGYQ IGFGNCEGTI
     LPADKRQ
 
 
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