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P35505

- FAAA_MOUSE

UniProt

P35505 - FAAA_MOUSE

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

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 acceptor Inferred
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. L-phenylalanine catabolic process Source: UniProtKB-UniPathway
  2. arginine catabolic process Source: MGI
  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

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 – 11Removed By similarity
Chaini2 – 419418Fumarylacetoacetase
PRO_0000156826Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By 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.

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP35505.

Family & Domainsi

Sequence similaritiesi

Belongs to the FAH family.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1302SS → PF in CAA77819. 1 Publication
Sequence conflicti307 – 3071G → R no nucleotide entry 1 Publication
Sequence conflicti376 – 3761E → G in AAA37591. 1 Publication
Sequence conflicti376 – 3761E → G in AAH10767. 1 Publication

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

« 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(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: July 9, 2014
This is version 121 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

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