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P35505

- FAAA_MOUSE

UniProt

P35505 - FAAA_MOUSE

Protein

Fumarylacetoacetase

Gene

Fah

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    4-fumarylacetoacetate + H2O = acetoacetate + fumarate.

    Cofactori

    Calcium.
    Magnesium.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi126 – 1261Calcium
    Binding sitei128 – 1281Substrate
    Active sitei133 – 1331Proton acceptorCurated
    Binding sitei142 – 1421Substrate
    Metal bindingi199 – 1991Calcium
    Metal bindingi201 – 2011Calcium
    Metal bindingi233 – 2331Calcium
    Metal bindingi233 – 2331Magnesium
    Binding sitei240 – 2401Substrate
    Binding sitei244 – 2441Substrate
    Metal bindingi253 – 2531Magnesium
    Metal bindingi257 – 2571Magnesium
    Binding sitei350 – 3501Substrate

    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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Phenylalanine catabolism, Tyrosine catabolism

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00139; UER00341.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarylacetoacetase (EC:3.7.1.2)
    Short name:
    FAA
    Alternative name(s):
    Beta-diketonase
    Fumarylacetoacetate hydrolase
    Gene namesi
    Name:Fah
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:95482. Fah.

    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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP35505.
    PaxDbiP35505.
    PRIDEiP35505.

    2D gel databases

    SWISS-2DPAGEP35505.

    PTM databases

    PhosphoSiteiP35505.

    Expressioni

    Tissue specificityi

    Mainly in liver and kidney.

    Gene expression databases

    ArrayExpressiP35505.
    BgeeiP35505.
    CleanExiMM_FAH.
    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 – 43
    Turni14 – 163
    Beta strandi19 – 235
    Beta strandi31 – 366
    Beta strandi39 – 424
    Turni43 – 464
    Helixi47 – 493
    Turni53 – 575
    Helixi59 – 635
    Beta strandi64 – 674
    Helixi68 – 736
    Helixi75 – 8915
    Turni90 – 945
    Helixi95 – 984
    Helixi100 – 1067
    Beta strandi107 – 1104
    Beta strandi114 – 1163
    Beta strandi124 – 1274
    Helixi131 – 14212
    Helixi144 – 1463
    Turni150 – 1545
    Beta strandi158 – 1603
    Beta strandi166 – 1683
    Beta strandi177 – 1804
    Beta strandi189 – 1924
    Beta strandi199 – 2068
    Helixi218 – 2214
    Helixi222 – 2243
    Beta strandi225 – 2328
    Helixi237 – 2437
    Turni245 – 2473
    Helixi251 – 2544
    Beta strandi257 – 2593
    Beta strandi263 – 2653
    Helixi266 – 2694
    Helixi270 – 2723
    Helixi285 – 2873
    Beta strandi298 – 3047
    Beta strandi312 – 3187
    Helixi319 – 3213
    Helixi326 – 3349
    Beta strandi345 – 3473
    Helixi356 – 3583
    Helixi362 – 3654
    Turni366 – 3705
    Beta strandi373 – 3764
    Beta strandi380 – 3834
    Beta strandi389 – 3979
    Beta strandi402 – 41312

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    InParanoidiQ3TY87.
    KOiK01555.
    OMAiFVGPGNK.
    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

    MSFIPVAEDS DFPIQNLPYG VFSTQSNPKP RIGVAIGDQI LDLSVIKHLF    50
    TGPALSKHQH VFDETTLNNF MGLGQAAWKE ARASLQNLLS ASQARLRDDK 100
    ELRQRAFTSQ ASATMHLPAT IGDYTDFYSS RQHATNVGIM FRGKENALLP 150
    NWLHLPVGYH GRASSIVVSG TPIRRPMGQM RPDNSKPPVY GACRLLDMEL 200
    EMAFFVGPGN RFGEPIPISK AHEHIFGMVL MNDWSARDIQ QWEYVPLGPF 250
    LGKSFGTTIS PWVVPMDALM PFVVPNPKQD PKPLPYLCHS QPYTFDINLS 300
    VSLKGEGMSQ AATICRSNFK HMYWTMLQQL THHSVNGCNL RPGDLLASGT 350
    ISGSDPESFG SMLELSWKGT KAIDVEQGQT RTFLLDGDEV IITGHCQGDG 400
    YRVGFGQCAG KVLPALSPA 419
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS21418.1.
    PIRi A40219.
    A56825.
    RefSeqi NP_034306.2. NM_010176.4.
    UniGenei Mm.3798.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HYO X-ray 1.30 A/B 1-419 [» ]
    1QCN X-ray 1.90 A/B 1-419 [» ]
    1QCO X-ray 1.90 A/B 1-419 [» ]
    1QQJ X-ray 1.55 A/B 1-419 [» ]
    2HZY X-ray 1.35 A/B 1-419 [» ]
    ProteinModelPortali P35505.
    SMRi P35505. Positions 1-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P35505. 6 interactions.
    MINTi MINT-1854354.
    STRINGi 10090.ENSMUSP00000032865.

    PTM databases

    PhosphoSitei P35505.

    2D gel databases

    SWISS-2DPAGE P35505.

    Proteomic databases

    MaxQBi P35505.
    PaxDbi P35505.
    PRIDEi P35505.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032865 ; ENSMUSP00000032865 ; ENSMUSG00000030630 .
    GeneIDi 14085.
    KEGGi mmu:14085.
    UCSCi uc009iej.3. mouse.

    Organism-specific databases

    CTDi 2184.
    MGIi MGI:95482. Fah.

    Phylogenomic databases

    eggNOGi COG0179.
    GeneTreei ENSGT00390000008646.
    HOGENOMi HOG000256845.
    HOVERGENi HBG001919.
    InParanoidi Q3TY87.
    KOi K01555.
    OMAi FVGPGNK.
    OrthoDBi EOG7TBC21.
    TreeFami TF315211.

    Enzyme and pathway databases

    UniPathwayi UPA00139 ; UER00341 .

    Miscellaneous databases

    EvolutionaryTracei P35505.
    NextBioi 285108.
    PROi P35505.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35505.
    Bgeei P35505.
    CleanExi MM_FAH.
    Genevestigatori P35505.

    Family and domain databases

    Gene3Di 2.30.30.230. 1 hit.
    3.90.850.10. 1 hit.
    InterProi IPR005959. Fumarylacetoacetase.
    IPR002529. Fumarylacetoacetase_C.
    IPR011234. Fumarylacetoacetase_C-rel.
    IPR015377. Fumarylacetoacetase_N.
    [Graphical view ]
    PANTHERi PTHR11820:SF1. PTHR11820:SF1. 1 hit.
    Pfami PF01557. FAA_hydrolase. 1 hit.
    PF09298. FAA_hydrolase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56529. SSF56529. 1 hit.
    SSF63433. SSF63433. 1 hit.
    TIGRFAMsi TIGR01266. fum_ac_acetase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    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: October 1, 2014
    This is version 122 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