FAAA_EMENI
ID FAAA_EMENI Reviewed; 431 AA.
AC Q00770; C8VKJ7; O42828; Q5BC34;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Fumarylacetoacetase;
DE Short=FAA;
DE EC=3.7.1.2 {ECO:0000269|PubMed:7568087};
DE AltName: Full=Beta-diketonase;
DE AltName: Full=Fumarylacetoacetate hydrolase;
GN Name=fahA; Synonyms=fah; ORFNames=AN1896;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION,
RP AND MISCELLANEOUS.
RC STRAIN=biA1;
RX PubMed=7568087; DOI=10.1073/pnas.92.20.9132;
RA Fernandez-Canon J.M., Penalva M.A.;
RT "Fungal metabolic model for human type I hereditary tyrosinaemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9132-9136(1995).
RN [2]
RP SEQUENCE REVISION TO 67-68, AND PROBABLE FUNCTION.
RC STRAIN=biA1;
RX PubMed=9417084; DOI=10.1074/jbc.273.1.329;
RA Fernandez-Canon J.M., Penalva M.A.;
RT "Characterization of a fungal maleylacetoacetate isomerase gene and
RT identification of its human homologue.";
RL J. Biol. Chem. 273:329-337(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Use of phenylalanine and phenylacetate as a carbon source.
CC {ECO:0000269|PubMed:7568087}.
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:7568087};
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 -!- INDUCTION: By phenylacetate (PhoAc), 2OH-PhoAc, 3OH-PhoAc, 4OH-PhoAc,
CC phenylalanine, and tyrosine. Not induced by acetate or glutamate.
CC Expression is partially repressed by glucose.
CC {ECO:0000269|PubMed:7568087}.
CC -!- MISCELLANEOUS: Disruption of the fahA gene results in phenylalanine
CC toxicity, secretion of succinylacetone and the absence of growth. This
CC is analogous to the genetic disease, type I hereditary tyrosinemia in
CC humans. {ECO:0000305|PubMed:7568087}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR EMBL; L41670; AAA85778.1; -; Genomic_DNA.
DR EMBL; AJ001836; CAA05043.1; -; Genomic_DNA.
DR EMBL; AACD01000029; EAA65061.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF85777.1; -; Genomic_DNA.
DR RefSeq; XP_659500.1; XM_654408.1.
DR AlphaFoldDB; Q00770; -.
DR SMR; Q00770; -.
DR STRING; 162425.CADANIAP00008552; -.
DR PRIDE; Q00770; -.
DR EnsemblFungi; CBF85777; CBF85777; ANIA_01896.
DR EnsemblFungi; EAA65061; EAA65061; AN1896.2.
DR GeneID; 2874818; -.
DR KEGG; ani:AN1896.2; -.
DR VEuPathDB; FungiDB:AN1896; -.
DR eggNOG; KOG2843; Eukaryota.
DR HOGENOM; CLU_026207_2_0_1; -.
DR InParanoid; Q00770; -.
DR OMA; YWTAAQQ; -.
DR OrthoDB; 980065at2759; -.
DR BioCyc; MetaCyc:MON-12048; -.
DR UniPathway; UPA00139; UER00341.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004334; F:fumarylacetoacetase activity; IMP:AspGD.
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; IDA:AspGD.
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 1: Evidence at protein level;
KW Calcium; Hydrolase; Magnesium; Metal-binding; Phenylalanine catabolism;
KW Reference proteome; Tyrosine catabolism.
FT CHAIN 1..431
FT /note="Fumarylacetoacetase"
FT /id="PRO_0000156828"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P35505"
FT CONFLICT 67..68
FT /note="NQ -> KE (in Ref. 2; CAA05043)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="H -> R (in Ref. 1; AAA85778 and 2; CAA05043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 46977 MW; A0757E4FDEEFB190 CRC64;
MASWLQIPKN SPFSLANIPF GIISSSKLSS RVPAIAIGDY ALDLSKFASS GGFSQLPVIQ
PHLNVFNQST LNAFAALGRP VHRQVREYIQ KVFSTETPFP QILRDNAALQ KEALLPLSEV
TNHLPMQIGD YTDFYAGLNH AYNVGVLFRG PDNALQPNYK HLPVAYHGRA SSVVTSGTPL
HRPQGQILTN PAANPKLPTF SPCKKLDIEL ELAFFVSTPN DLGHPVHIDK AEDHIFGVVL
MNDWSARDIQ AWEYVPLGPF NAKNFGTTIT PWVVLIDALE PFRTVGLEPG NRESLLPYLR
EKRADTAYDI PLEVEVTNAG GEPTVISHSN AKNLLYSFPQ MLAHHTITGC NLNTGDLLGS
GTISGKENQT EGSFLEQTNG KNPIKLADGS ERLFLEDGDT VILRGMAGTE GNYVGFGDCA
GTILPPVQLD L
