Reviewed, UniProtKB/Swiss-Prot Q00770 (FAAA_EMENI)

Names and origin

Protein names

Recommended name:
    Fumarylacetoacetase
      Short name=FAA
    EC=3.7.1.2
Alternative name(s):
    Fumarylacetoacetate hydrolase
    Beta-diketonase

Gene names

Name:	fahA
Synonyms:	fah
ORF Names:	AN1896

Organism

Emericella nidulans (Aspergillus nidulans) [Complete proteome]

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Use of phenylalanine and phenylacetate as a carbon source. Ref.2
Catalytic activity	4-fumarylacetoacetate + H2O = acetoacetate + fumarate.
Cofactor	Calcium By similarity. Magnesium By similarity.
Pathway	Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 6/6.
Induction	By phenylacetate (PhoAc), 2OH-PhoAc, 3OH-PhoAc, 4OH-PhoAc, phenylalanine, and tyrosine. Not induced by acetate or glutamate. Expression is partially repressed by glucose.
Miscellaneous	Disruption of the fah gene results in phenylalanine toxicity, secretion of succinylacetone and the absence of growth. This is analogous to the genetic disease, type I hereditary tyrosinaemia in humans.
Sequence similarities	Belongs to the FAH family.

Ontologies

Keywords
Biological process	Phenylalanine catabolism Tyrosine catabolism
Ligand	Calcium Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	L-phenylalanine catabolic process Inferred from electronic annotation. Source: UniProtKB-KW tyrosine catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW fumarylacetoacetase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 431	431	Fumarylacetoacetase		PRO_0000156828
Sites
	Active site	140	1	Proton acceptor Probable
	Metal binding	133	1	Calcium By similarity
	Metal binding	209	1	Calcium By similarity
	Metal binding	211	1	Calcium By similarity
	Metal binding	243	1	Calcium By similarity
	Metal binding	243	1	Magnesium By similarity
	Metal binding	263	1	Magnesium By similarity
	Metal binding	267	1	Magnesium By similarity
	Binding site	135	1	Substrate By similarity
	Binding site	149	1	Substrate By similarity
	Binding site	250	1	Substrate By similarity
	Binding site	254	1	Substrate By similarity
	Binding site	362	1	Substrate By similarity
Experimental info
	Sequence conflict	67 – 68	2	NQ → KE in CAA05043. Ref.2
	Sequence conflict	328	1	H → R in AAA85778. Ref.1
	Sequence conflict	328	1	H → R in CAA05043. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q00770-1 [UniParc]. Last modified May 26, 2009. Version 3. Checksum: A0757E4FDEEFB190	FASTA	431	46,977
	10 20 30 40 50 60 MASWLQIPKN SPFSLANIPF GIISSSKLSS RVPAIAIGDY ALDLSKFASS GGFSQLPVIQ 70 80 90 100 110 120 PHLNVFNQST LNAFAALGRP VHRQVREYIQ KVFSTETPFP QILRDNAALQ KEALLPLSEV 130 140 150 160 170 180 TNHLPMQIGD YTDFYAGLNH AYNVGVLFRG PDNALQPNYK HLPVAYHGRA SSVVTSGTPL 190 200 210 220 230 240 HRPQGQILTN PAANPKLPTF SPCKKLDIEL ELAFFVSTPN DLGHPVHIDK AEDHIFGVVL 250 260 270 280 290 300 MNDWSARDIQ AWEYVPLGPF NAKNFGTTIT PWVVLIDALE PFRTVGLEPG NRESLLPYLR 310 320 330 340 350 360 EKRADTAYDI PLEVEVTNAG GEPTVISHSN AKNLLYSFPQ MLAHHTITGC NLNTGDLLGS 370 380 390 400 410 420 GTISGKENQT EGSFLEQTNG KNPIKLADGS ERLFLEDGDT VILRGMAGTE GNYVGFGDCA 430 GTILPPVQLD L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Fungal metabolic model for human type I hereditary tyrosinaemia." Fernandez-Canon J.M., Penalva M.A. Proc. Natl. Acad. Sci. U.S.A. 92:9132-9136(1995) [PubMed: 7568087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: biA1.
[2]	"Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue." Fernandez-Canon J.M., Penalva M.A. J. Biol. Chem. 273:329-337(1998) [PubMed: 9417084] [Abstract] Cited for: SEQUENCE REVISION TO 67-68, PROBABLE FUNCTION. Strain: biA1.
[3]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L41670 Genomic DNA. Translation: AAA85778.1. AJ001836 Genomic DNA. Translation: CAA05043.1. AACD01000029 Genomic DNA. Translation: EAA65061.1.
RefSeq	XP_659500.1.
3D structure databases
HSSP	HSSP built from PDB template 1HYO based on UniProtKB P35505.
ModBase	Search...
Genome annotation databases
GeneID	2874818.
KEGG	ani:AN1896.2.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-12048.
BRENDA	3.7.1.2. 3859.
Family and domain databases
InterPro	IPR005959. Fumarylacetoacetase. IPR002529. Fumarylacetoacetase_C-like. IPR011234. Fumarylacetoacetase_C-rel. IPR015377. Fumarylacetoacetase_N. [Graphical view]
Gene3D	G3DSA:3.90.850.10. Fumarylacetoacetase_C-rel. 1 hit. G3DSA:2.30.30.230. Fumarylacetoacetase_N. 1 hit.
PANTHER	PTHR11820:SF1. Fum_ac_acetase. 1 hit.
Pfam	PF09298. DUF1969. 1 hit. PF01557. FAA_hydrolase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01266. fum_ac_acetase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FAAA_EMENI

Accession

Primary (citable) accession number: Q00770
Secondary accession number(s): O42828, Q5BC34

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	May 26, 2009
Last modified:	September 22, 2009
This is version 51 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)