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Protein

Fumarylacetoacetase

Gene

Fah

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

4-fumarylacetoacetate + H2O = acetoacetate + fumarate.2 Publications

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi126 – 1261Calcium2 Publications
Binding sitei128 – 1281Substrate1 Publication
Active sitei133 – 1331Proton acceptor1 Publication
Binding sitei142 – 1421Substrate1 Publication
Metal bindingi199 – 1991Calcium2 Publications
Metal bindingi201 – 2011Calcium2 Publications
Metal bindingi233 – 2331Calcium2 Publications
Metal bindingi233 – 2331Magnesium1 Publication
Binding sitei240 – 2401Substrate1 Publication
Binding sitei244 – 2441Substrate1 Publication
Metal bindingi253 – 2531Magnesium1 Publication
Metal bindingi257 – 2571Magnesium1 Publication
Binding sitei350 – 3501Substrate1 Publication

GO - Molecular functioni

  1. fumarylacetoacetase activity Source: MGI
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine catabolic process Source: MGI
  2. L-phenylalanine catabolic process Source: UniProtKB-UniPathway
  3. tyrosine catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Phenylalanine catabolism, Tyrosine catabolism

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.7.1.2. 3474.
ReactomeiREACT_336040. Phenylalanine and tyrosine catabolism.
UniPathwayiUPA00139; UER00341.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarylacetoacetase (EC:3.7.1.22 Publications)
Short name:
FAA
Alternative name(s):
Beta-diketonase
Fumarylacetoacetate hydrolase
Gene namesi
Name:Fah
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:95482. Fah.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi201 – 2011E → G: Decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 419418FumarylacetoacetasePRO_0000156826Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei309 – 3091PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP35505.
PaxDbiP35505.
PRIDEiP35505.

2D gel databases

SWISS-2DPAGEP35505.

PTM databases

PhosphoSiteiP35505.

Expressioni

Tissue specificityi

Mainly in liver and kidney.

Gene expression databases

BgeeiP35505.
CleanExiMM_FAH.
ExpressionAtlasiP35505. baseline and differential.
GenevestigatoriP35505.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

IntActiP35505. 6 interactions.
MINTiMINT-1854354.
STRINGi10090.ENSMUSP00000032865.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Turni14 – 163Combined sources
Beta strandi19 – 235Combined sources
Beta strandi31 – 366Combined sources
Beta strandi39 – 424Combined sources
Turni43 – 464Combined sources
Helixi47 – 493Combined sources
Turni53 – 575Combined sources
Helixi59 – 635Combined sources
Beta strandi64 – 674Combined sources
Helixi68 – 736Combined sources
Helixi75 – 8915Combined sources
Turni90 – 945Combined sources
Helixi95 – 984Combined sources
Helixi100 – 1067Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi124 – 1274Combined sources
Helixi131 – 14212Combined sources
Helixi144 – 1463Combined sources
Turni150 – 1545Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi177 – 1804Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi199 – 2068Combined sources
Helixi218 – 2214Combined sources
Helixi222 – 2243Combined sources
Beta strandi225 – 2328Combined sources
Helixi237 – 2437Combined sources
Turni245 – 2473Combined sources
Helixi251 – 2544Combined sources
Beta strandi257 – 2593Combined sources
Beta strandi263 – 2653Combined sources
Helixi266 – 2694Combined sources
Helixi270 – 2723Combined sources
Helixi285 – 2873Combined sources
Beta strandi298 – 3047Combined sources
Beta strandi312 – 3187Combined sources
Helixi319 – 3213Combined sources
Helixi326 – 3349Combined sources
Beta strandi345 – 3473Combined sources
Helixi356 – 3583Combined sources
Helixi362 – 3654Combined sources
Turni366 – 3705Combined sources
Beta strandi373 – 3764Combined sources
Beta strandi380 – 3834Combined sources
Beta strandi389 – 3979Combined sources
Beta strandi402 – 41312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP35505.
SMRiP35505. Positions 1-417.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35505.

Family & Domainsi

Sequence similaritiesi

Belongs to the FAH family.Curated

Phylogenomic databases

eggNOGiCOG0179.
GeneTreeiENSGT00390000008646.
HOGENOMiHOG000256845.
HOVERGENiHBG001919.
InParanoidiP35505.
KOiK01555.
OMAiLSWKGTK.
OrthoDBiEOG7TBC21.
TreeFamiTF315211.

Family and domain databases

Gene3Di2.30.30.230. 1 hit.
3.90.850.10. 1 hit.
InterProiIPR005959. Fumarylacetoacetase.
IPR002529. Fumarylacetoacetase_C.
IPR011234. Fumarylacetoacetase_C-rel.
IPR015377. Fumarylacetoacetase_N.
[Graphical view]
PANTHERiPTHR11820:SF1. PTHR11820:SF1. 1 hit.
PfamiPF01557. FAA_hydrolase. 1 hit.
PF09298. FAA_hydrolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56529. SSF56529. 1 hit.
SSF63433. SSF63433. 1 hit.
TIGRFAMsiTIGR01266. fum_ac_acetase. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35505-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFIPVAEDS DFPIQNLPYG VFSTQSNPKP RIGVAIGDQI LDLSVIKHLF
60 70 80 90 100
TGPALSKHQH VFDETTLNNF MGLGQAAWKE ARASLQNLLS ASQARLRDDK
110 120 130 140 150
ELRQRAFTSQ ASATMHLPAT IGDYTDFYSS RQHATNVGIM FRGKENALLP
160 170 180 190 200
NWLHLPVGYH GRASSIVVSG TPIRRPMGQM RPDNSKPPVY GACRLLDMEL
210 220 230 240 250
EMAFFVGPGN RFGEPIPISK AHEHIFGMVL MNDWSARDIQ QWEYVPLGPF
260 270 280 290 300
LGKSFGTTIS PWVVPMDALM PFVVPNPKQD PKPLPYLCHS QPYTFDINLS
310 320 330 340 350
VSLKGEGMSQ AATICRSNFK HMYWTMLQQL THHSVNGCNL RPGDLLASGT
360 370 380 390 400
ISGSDPESFG SMLELSWKGT KAIDVEQGQT RTFLLDGDEV IITGHCQGDG
410
YRVGFGQCAG KVLPALSPA
Length:419
Mass (Da):46,176
Last modified:July 27, 2011 - v2
Checksum:i771C247377B59102
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1302SS → PF in CAA77819 (PubMed:1524868).Curated
Sequence conflicti307 – 3071G → R no nucleotide entry (PubMed:1644288).Curated
Sequence conflicti376 – 3761E → G in AAA37591 (PubMed:1741389).Curated
Sequence conflicti376 – 3761E → G in AAH10767 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21418.1.
PIRiA40219.
A56825.
RefSeqiNP_034306.2. NM_010176.4.
UniGeneiMm.3798.

Genome annotation databases

EnsembliENSMUST00000032865; ENSMUSP00000032865; ENSMUSG00000030630.
GeneIDi14085.
KEGGimmu:14085.
UCSCiuc009iej.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21418.1.
PIRiA40219.
A56825.
RefSeqiNP_034306.2. NM_010176.4.
UniGeneiMm.3798.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP35505.
SMRiP35505. Positions 1-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP35505. 6 interactions.
MINTiMINT-1854354.
STRINGi10090.ENSMUSP00000032865.

PTM databases

PhosphoSiteiP35505.

2D gel databases

SWISS-2DPAGEP35505.

Proteomic databases

MaxQBiP35505.
PaxDbiP35505.
PRIDEiP35505.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032865; ENSMUSP00000032865; ENSMUSG00000030630.
GeneIDi14085.
KEGGimmu:14085.
UCSCiuc009iej.3. mouse.

Organism-specific databases

CTDi2184.
MGIiMGI:95482. Fah.

Phylogenomic databases

eggNOGiCOG0179.
GeneTreeiENSGT00390000008646.
HOGENOMiHOG000256845.
HOVERGENiHBG001919.
InParanoidiP35505.
KOiK01555.
OMAiLSWKGTK.
OrthoDBiEOG7TBC21.
TreeFamiTF315211.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00341.
BRENDAi3.7.1.2. 3474.
ReactomeiREACT_336040. Phenylalanine and tyrosine catabolism.

Miscellaneous databases

EvolutionaryTraceiP35505.
NextBioi285108.
PROiP35505.
SOURCEiSearch...

Gene expression databases

BgeeiP35505.
CleanExiMM_FAH.
ExpressionAtlasiP35505. baseline and differential.
GenevestigatoriP35505.

Family and domain databases

Gene3Di2.30.30.230. 1 hit.
3.90.850.10. 1 hit.
InterProiIPR005959. Fumarylacetoacetase.
IPR002529. Fumarylacetoacetase_C.
IPR011234. Fumarylacetoacetase_C-rel.
IPR015377. Fumarylacetoacetase_N.
[Graphical view]
PANTHERiPTHR11820:SF1. PTHR11820:SF1. 1 hit.
PfamiPF01557. FAA_hydrolase. 1 hit.
PF09298. FAA_hydrolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56529. SSF56529. 1 hit.
SSF63433. SSF63433. 1 hit.
TIGRFAMsiTIGR01266. fum_ac_acetase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1991) [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(1991) [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(1991) [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.
    , 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(2004) [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(2003) [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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-201, CATALYTIC ACTIVITY.
  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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PRODUCTS AND CALCIUM, COFACTOR, ACTIVE SITE, SUBUNIT.
  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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH INHIBITOR; CALCIUM AND MAGNESIUM, SUBUNIT, CATALYTIC ACTIVITY, COFACTOR.

Entry informationi

Entry nameiFAAA_MOUSE
AccessioniPrimary (citable) accession number: P35505
Secondary accession number(s): Q3TY87, Q9QW65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.