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P35505 (FAAA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fumarylacetoacetase

Short name=FAA
EC=3.7.1.2
Alternative name(s):
Beta-diketonase
Fumarylacetoacetate hydrolase
Gene names
Name:Fah
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

4-fumarylacetoacetate + H2O = acetoacetate + fumarate.

Cofactor

Calcium.

Magnesium.

Pathway

Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 6/6.

Subunit structure

Homodimer.

Tissue specificity

Mainly in liver and kidney.

Sequence similarities

Belongs to the FAH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 419418Fumarylacetoacetase
PRO_0000156826

Sites

Active site1331Proton acceptor Probable
Metal binding1261Calcium
Metal binding1991Calcium
Metal binding2011Calcium
Metal binding2331Calcium
Metal binding2331Magnesium
Metal binding2531Magnesium
Metal binding2571Magnesium
Binding site1281Substrate
Binding site1421Substrate
Binding site2401Substrate
Binding site2441Substrate
Binding site3501Substrate

Amino acid modifications

Modified residue21N-acetylserine By similarity

Experimental info

Mutagenesis2011E → G: Decrease in activity. Ref.6
Sequence conflict129 – 1302SS → PF in CAA77819. Ref.2
Sequence conflict3071G → R no nucleotide entry Ref.3
Sequence conflict3761E → G in AAA37591. Ref.1
Sequence conflict3761E → G in AAH10767. Ref.5

Secondary structure

...................................................................................... 419
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35505 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 771C247377B59102

FASTA41946,176
        10         20         30         40         50         60 
MSFIPVAEDS DFPIQNLPYG VFSTQSNPKP RIGVAIGDQI LDLSVIKHLF TGPALSKHQH 

        70         80         90        100        110        120 
VFDETTLNNF MGLGQAAWKE ARASLQNLLS ASQARLRDDK ELRQRAFTSQ ASATMHLPAT 

       130        140        150        160        170        180 
IGDYTDFYSS RQHATNVGIM FRGKENALLP NWLHLPVGYH GRASSIVVSG TPIRRPMGQM 

       190        200        210        220        230        240 
RPDNSKPPVY GACRLLDMEL EMAFFVGPGN RFGEPIPISK AHEHIFGMVL MNDWSARDIQ 

       250        260        270        280        290        300 
QWEYVPLGPF LGKSFGTTIS PWVVPMDALM PFVVPNPKQD PKPLPYLCHS QPYTFDINLS 

       310        320        330        340        350        360 
VSLKGEGMSQ AATICRSNFK HMYWTMLQQL THHSVNGCNL RPGDLLASGT ISGSDPESFG 

       370        380        390        400        410 
SMLELSWKGT KAIDVEQGQT RTFLLDGDEV IITGHCQGDG YRVGFGQCAG KVLPALSPA 

« Hide

References

« Hide 'large scale' references
[1]"Murine fumarylacetoacetate hydrolase (Fah) gene is disrupted by a neonatally lethal albino deletion that defines the hepatocyte-specific developmental regulation 1 (hsdr-1) locus."
Klebig M.L., Russell L.B., Rinchik E.M.
Proc. Natl. Acad. Sci. U.S.A. 89:1363-1367(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence of a cDNA encoding murine fumarylacetoacetate hydrolase."
Grompe M., Al-Dhalimy M.
Biochem. Med. Metab. Biol. 48:26-31(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Liver.
[3]"Deficiency of an enzyme of tyrosine metabolism underlies altered gene expression in newborn liver of lethal albino mice."
Ruppert S., Kelsey G., Schedl A., Schmid E., Thies E., Schutz G.
Genes Dev. 6:1430-1443(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Spleen and Visual cortex.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[6]"Point mutations in the murine fumarylacetoacetate hydrolase gene: animal models for the human genetic disorder hereditary tyrosinemia type 1."
Aponte J.L., Sega G.A., Hauser L.J., Dhar M.S., Withrow C.M., Carpenter D.A., Rinchik E.M., Culiat C.T., Johnson D.K.
Proc. Natl. Acad. Sci. U.S.A. 98:641-645(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-201.
[7]"Crystal structure and mechanism of a carbon-carbon bond hydrolase."
Timm D.E., Mueller H.A., Bhanumoorthy P., Harp J.M., Bunick G.J.
Structure 7:1023-1033(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PRODUCTS AND DIVALENT METAL CATIONS.
[8]"Mechanistic inferences from the crystal structure of fumarylacetoacetate hydrolase with a bound phosphorus-based inhibitor."
Bateman R.L., Bhanumoorthy P., Witte J.F., McClard R.W., Grompe M., Timm D.E.
J. Biol. Chem. 276:15284-15291(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH INHIBITOR AND METAL IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84145 mRNA. Translation: AAA37591.1.
Z11774 mRNA. Translation: CAA77819.1.
AK143759 mRNA. Translation: BAE25527.1.
AK158808 mRNA. Translation: BAE34676.1.
BC010767 mRNA. Translation: AAH10767.1.
CCDSCCDS21418.1.
PIRA40219.
A56825.
RefSeqNP_034306.2. NM_010176.4.
UniGeneMm.3798.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HYOX-ray1.30A/B1-419[»]
1QCNX-ray1.90A/B1-419[»]
1QCOX-ray1.90A/B1-419[»]
1QQJX-ray1.55A/B1-419[»]
2HZYX-ray1.35A/B1-419[»]
ProteinModelPortalP35505.
SMRP35505. Positions 1-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP35505. 6 interactions.
MINTMINT-1854354.
STRING10090.ENSMUSP00000032865.

PTM databases

PhosphoSiteP35505.

2D gel databases

SWISS-2DPAGEP35505.

Proteomic databases

MaxQBP35505.
PaxDbP35505.
PRIDEP35505.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032865; ENSMUSP00000032865; ENSMUSG00000030630.
GeneID14085.
KEGGmmu:14085.
UCSCuc009iej.3. mouse.

Organism-specific databases

CTD2184.
MGIMGI:95482. Fah.

Phylogenomic databases

eggNOGCOG0179.
GeneTreeENSGT00390000008646.
HOGENOMHOG000256845.
HOVERGENHBG001919.
InParanoidQ3TY87.
KOK01555.
OMAFVGPGNK.
OrthoDBEOG7TBC21.
TreeFamTF315211.

Enzyme and pathway databases

UniPathwayUPA00139; UER00341.

Gene expression databases

ArrayExpressP35505.
BgeeP35505.
CleanExMM_FAH.
GenevestigatorP35505.

Family and domain databases

Gene3D2.30.30.230. 1 hit.
3.90.850.10. 1 hit.
InterProIPR005959. Fumarylacetoacetase.
IPR002529. Fumarylacetoacetase_C.
IPR011234. Fumarylacetoacetase_C-rel.
IPR015377. Fumarylacetoacetase_N.
[Graphical view]
PANTHERPTHR11820:SF1. PTHR11820:SF1. 1 hit.
PfamPF01557. FAA_hydrolase. 1 hit.
PF09298. FAA_hydrolase_N. 1 hit.
[Graphical view]
SUPFAMSSF56529. SSF56529. 1 hit.
SSF63433. SSF63433. 1 hit.
TIGRFAMsTIGR01266. fum_ac_acetase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP35505.
NextBio285108.
PROP35505.
SOURCESearch...

Entry information

Entry nameFAAA_MOUSE
AccessionPrimary (citable) accession number: P35505
Secondary accession number(s): Q3TY87, Q9QW65
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot