ID A1DFK1_NEOFI Unreviewed; 431 AA.
AC A1DFK1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=Fumarylacetoacetase {ECO:0000256|ARBA:ARBA00012094, ECO:0000256|RuleBase:RU366008};
DE EC=3.7.1.2 {ECO:0000256|ARBA:ARBA00012094, ECO:0000256|RuleBase:RU366008};
DE AltName: Full=Fumarylacetoacetate hydrolase {ECO:0000256|RuleBase:RU366008};
GN ORFNames=NFIA_081020 {ECO:0000313|EMBL:EAW18158.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW18158.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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:0000256|RuleBase:RU366008};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU366008};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU366008};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 6/6.
CC {ECO:0000256|ARBA:ARBA00004782, ECO:0000256|RuleBase:RU366008}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000256|ARBA:ARBA00010211,
CC ECO:0000256|RuleBase:RU366008}.
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DR EMBL; DS027696; EAW18158.1; -; Genomic_DNA.
DR RefSeq; XP_001260055.1; XM_001260054.1.
DR AlphaFoldDB; A1DFK1; -.
DR STRING; 331117.A1DFK1; -.
DR EnsemblFungi; EAW18158; EAW18158; NFIA_081020.
DR GeneID; 4586611; -.
DR KEGG; nfi:NFIA_081020; -.
DR VEuPathDB; FungiDB:NFIA_081020; -.
DR eggNOG; KOG2843; Eukaryota.
DR HOGENOM; CLU_026207_2_0_1; -.
DR OMA; YWTAAQQ; -.
DR OrthoDB; 275827at2759; -.
DR UniPathway; UPA00139; UER00341.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0004334; F:fumarylacetoacetase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.30.230; Fumarylacetoacetase, N-terminal domain; 1.
DR Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 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 NCBIfam; TIGR01266; fum_ac_acetase; 1.
DR PANTHER; PTHR43069; FUMARYLACETOACETASE; 1.
DR PANTHER; PTHR43069:SF2; FUMARYLACETOACETASE; 1.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR Pfam; PF09298; FAA_hydrolase_N; 1.
DR SUPFAM; SSF56529; FAH; 1.
DR SUPFAM; SSF63433; Fumarylacetoacetate hydrolase, FAH, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU366008};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366008};
KW Magnesium {ECO:0000256|RuleBase:RU366008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366008};
KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232,
KW ECO:0000256|RuleBase:RU366008};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878,
KW ECO:0000256|RuleBase:RU366008}.
FT DOMAIN 16..125
FT /note="Fumarylacetoacetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09298"
FT DOMAIN 139..410
FT /note="Fumarylacetoacetase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01557"
SQ SEQUENCE 431 AA; 46849 MW; F45A85630F6B19E3 CRC64;
MASWLQIPKN SPFSLANIPF GIISSAKVTS PVAAVAIGDY ALNLSIFASS GGFSQLPVIQ
PHLSVFGQPT LNAFAALGRP VHRQVREYIQ SIFRADTPFP QILKDNSTLQ KEALLPLSEV
TNHLPMHIGD YTDFYAGLNH AYNIGVLFRG PENALQPNYK HLPVGYHGRA SSVVTSGTPI
RRPNGQILAN PAANPKVPTF SPCKRLDIEL ELAAFVSKSN ELGQPVSIDE AEDHIFGVVL
MNDWSARDIQ AWEYVPLGPF NAKNFATTIT PWVVLLDALE PFRTAGLEPG NRESLLPYLR
EKRELNAYDI PLEVEITNAG GKPTLISRTN ANNLLYSFPQ MLAHHTITGC NMNTGDLLGS
GTISGKENQT QGSLLEQTNG KNPLKLADGS ERMFLEDGDT VVLRGMAGTE GNYVGFGDCV
GTILPALKLE F
//
