FAH_ARATH
ID FAH_ARATH Reviewed; 421 AA.
AC Q8RW90; O65374;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Fumarylacetoacetase {ECO:0000305};
DE EC=3.7.1.2 {ECO:0000269|PubMed:22980205};
DE AltName: Full=Fumarylacetoacetate hydrolase {ECO:0000303|PubMed:22980205};
DE Short=AtFAH {ECO:0000303|PubMed:22980205};
DE AltName: Full=Protein SHORT-DAY SENSITIVE CELL DEATH 1 {ECO:0000303|PubMed:23743712};
GN Name=FAH {ECO:0000303|PubMed:22980205};
GN Synonyms=SSCD1 {ECO:0000303|PubMed:23743712};
GN OrderedLocusNames=At1g12050 {ECO:0000312|Araport:AT1G12050};
GN ORFNames=F12F1.8 {ECO:0000312|EMBL:AAC17611.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22980205; DOI=10.1016/j.plantsci.2006.04.008;
RA Dixon D.P., Edwards R.;
RT "Enzymes of tyrosine catabolism in Arabidopsis thaliana.";
RL Plant Sci. 171:360-366(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23743712; DOI=10.1104/pp.113.216804;
RA Han C., Ren C., Zhi T., Zhou Z., Liu Y., Chen F., Peng W., Xie D.;
RT "Disruption of fumarylacetoacetate hydrolase causes spontaneous cell death
RT under short-day conditions in Arabidopsis.";
RL Plant Physiol. 162:1956-1964(2013).
RN [6]
RP FUNCTION.
RX PubMed=27097641; DOI=10.1007/s00425-016-2530-6;
RA Zhi T., Zhou Z., Huang Y., Han C., Liu Y., Zhu Q., Ren C.;
RT "Sugar suppresses cell death caused by disruption of fumarylacetoacetate
RT hydrolase in Arabidopsis.";
RL Planta 244:557-571(2016).
CC -!- FUNCTION: Converts fumarylacetoacetate to acetoacetate and fumarate
CC (PubMed:22980205). Involved in tyrosine catabolic pathway. Catalyzes
CC the final step in the tyrosine degradation pathway (PubMed:22980205,
CC PubMed:23743712, PubMed:27097641). {ECO:0000269|PubMed:22980205,
CC ECO:0000269|PubMed:23743712, ECO:0000269|PubMed:27097641}.
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:0000269|PubMed:22980205};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.7 uM for 4-fumarylacetoacetate {ECO:0000269|PubMed:22980205};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 6/6.
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Spontaneous cell death phenotype under short-day
CC conditions. {ECO:0000269|PubMed:23743712}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17611.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AC002131; AAC17611.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28830.1; -; Genomic_DNA.
DR EMBL; AY094010; AAM16166.1; -; mRNA.
DR PIR; F86255; F86255.
DR RefSeq; NP_172669.2; NM_101077.6.
DR AlphaFoldDB; Q8RW90; -.
DR SMR; Q8RW90; -.
DR STRING; 3702.AT1G12050.1; -.
DR PaxDb; Q8RW90; -.
DR PRIDE; Q8RW90; -.
DR ProteomicsDB; 222377; -.
DR EnsemblPlants; AT1G12050.1; AT1G12050.1; AT1G12050.
DR GeneID; 837757; -.
DR Gramene; AT1G12050.1; AT1G12050.1; AT1G12050.
DR KEGG; ath:AT1G12050; -.
DR Araport; AT1G12050; -.
DR TAIR; locus:2008845; AT1G12050.
DR eggNOG; KOG2843; Eukaryota.
DR HOGENOM; CLU_026207_2_0_1; -.
DR InParanoid; Q8RW90; -.
DR OMA; YWTAAQQ; -.
DR OrthoDB; 980065at2759; -.
DR PhylomeDB; Q8RW90; -.
DR BioCyc; ARA:AT1G12050-MON; -.
DR BRENDA; 3.7.1.2; 399.
DR UniPathway; UPA00139; UER00341.
DR PRO; PR:Q8RW90; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RW90; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0004334; F:fumarylacetoacetase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008219; P:cell death; IMP:TAIR.
DR GO; GO:1902000; P:homogentisate catabolic process; IDA:TAIR.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR GO; GO:0006572; P:tyrosine catabolic process; IGI:TAIR.
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 1: Evidence at protein level;
KW Calcium; Hydrolase; Magnesium; Metal-binding; Phenylalanine catabolism;
KW Reference proteome; Tyrosine catabolism.
FT CHAIN 1..421
FT /note="Fumarylacetoacetase"
FT /id="PRO_0000442048"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 147
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 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35505"
SQ SEQUENCE 421 AA; 46095 MW; 14F8458045893FAC CRC64;
MALLKSFIDV GSDSHFPIQN LPYGVFKPES NSTPRPAVAI GDLVLDLSAI SEAGLFDGLI
LKDADCFLQP NLNKFLAMGR PAWKEARSTL QRILSSNEPI LRDNDVLRRK SFHQMSKVEM
IVPMVIGDYT DFFASMHHAK NCGLMFRGPE NAINPNWFRL PIAYHGRASS IVISGTDIIR
PRGQGHPQGN SEPYFGPSKK LDFELEMAAV VGPGNELGKP IDVNNAADHI FGLLLMNDWS
ARDIQAWEYV PLGPFLGKSF GTTISPWIVT LDALEPFGCQ APKQDPPPLP YLAEKESVNY
DISLEVQLKP SGRDDSCVIT KSNFQNLYWT ITQQLAHHTV NGCNLRPGDL LGTGTISGPE
PDSYGCLLEL TWNGQKPLSL NGTTQTFLED GDQVTFSGVC KGDGYNVGFG TCTGKIVPSP
P
