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FAH_ORYSJ
ID   FAH_ORYSJ               Reviewed;         429 AA.
AC   Q6H7M1;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Fumarylacetoacetase {ECO:0000305};
DE            EC=3.7.1.2 {ECO:0000250|UniProtKB:Q8RW90};
DE   AltName: Full=Fumarylacetoacetate hydrolase {ECO:0000305};
GN   Name=FAH {ECO:0000305};
GN   OrderedLocusNames=Os02g0196800 {ECO:0000312|EMBL:BAF08109.1},
GN   LOC_Os02g10310 {ECO:0000305};
GN   ORFNames=OJ1524_D08.17 {ECO:0000312|EMBL:BAD25278.1},
GN   OsJ_05754 {ECO:0000312|EMBL:EAZ22093.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: Converts fumarylacetoacetate to acetoacetate and fumarate.
CC       Involved in tyrosine catabolic pathway. Catalyzes the final step in the
CC       tyrosine degradation pathway. {ECO:0000250|UniProtKB:Q8RW90}.
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:Q8RW90};
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       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR   EMBL; AP004191; BAD25278.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF08109.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS77461.1; -; Genomic_DNA.
DR   EMBL; CM000139; EAZ22093.1; -; Genomic_DNA.
DR   EMBL; AK070521; BAG92005.1; -; mRNA.
DR   RefSeq; XP_015622682.1; XM_015767196.1.
DR   AlphaFoldDB; Q6H7M1; -.
DR   SMR; Q6H7M1; -.
DR   STRING; 4530.OS02T0196800-01; -.
DR   PaxDb; Q6H7M1; -.
DR   PRIDE; Q6H7M1; -.
DR   EnsemblPlants; Os02t0196800-01; Os02t0196800-01; Os02g0196800.
DR   GeneID; 4328618; -.
DR   Gramene; Os02t0196800-01; Os02t0196800-01; Os02g0196800.
DR   KEGG; osa:4328618; -.
DR   eggNOG; KOG2843; Eukaryota.
DR   HOGENOM; CLU_026207_2_0_1; -.
DR   InParanoid; Q6H7M1; -.
DR   OMA; YWTAAQQ; -.
DR   OrthoDB; 980065at2759; -.
DR   PlantReactome; R-OSA-1119506; tyrosine degradation I.
DR   UniPathway; UPA00139; UER00341.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   ExpressionAtlas; Q6H7M1; baseline and differential.
DR   GO; GO:0004334; F:fumarylacetoacetase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008219; P:cell death; IEA:EnsemblPlants.
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   2: Evidence at transcript level;
KW   Calcium; Hydrolase; Magnesium; Metal-binding; Phenylalanine catabolism;
KW   Reference proteome; Tyrosine catabolism.
FT   CHAIN           1..429
FT                   /note="Fumarylacetoacetase"
FT                   /id="PRO_0000442049"
FT   ACT_SITE        146
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         139
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         212
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         214
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         246
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         266
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         270
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
FT   BINDING         363
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P35505"
SQ   SEQUENCE   429 AA;  47105 MW;  505E2F9DCADC0E53 CRC64;
     MAEGSRSPLR SFVEVAPGSH FPIQNLPFGV FRRRGSPEPE PPRPAVAIGD FALDLAAVSD
     AGLFHGPLLS ASPCFRQETL NMFLGMGRPA WKEARATLQK ILSADEPVLR DNEALKKKCL
     VPMSDTEMLL PITVGDYTDF FCSVHHARNC GFIFRGPQTP VNPNWFQLPV GYHGRASSVI
     VSGTDIIRPK GQGHPTGDSR PYFGPSKKLD FELEMAAIVG PGNELGKPID INDAEEHIFG
     LMIMNDWSAR DIQAWETIPL GPFLGKSFST TVSPWIVTMD ALKPFTCEAP KQEPEPLPYL
     AEKNHVNYDI PLEVWIKPKE QSEPSMVAKS NFKHLYWTLT QQLAHHTVNG CNLRPGDMFA
     TGTLSGPETE SLGCLLELTW NGQKEISVGN STRKFLEDGD EVILTACCKG EGYNVGFGTC
     TGKVLPALP
 
 
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