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P97807 (FUMH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fumarate hydratase, mitochondrial

Short name=Fumarase
EC=4.2.1.2
Alternative name(s):
EF-3
Gene names
Name:Fh
Synonyms:Fh1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-malate = fumarate + H2O. HAMAP-Rule MF_00743

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP-Rule MF_00743

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00743

Subcellular location

Isoform Mitochondrial: Mitochondrion HAMAP-Rule MF_00743.

Isoform Cytoplasmic: Cytoplasm HAMAP-Rule MF_00743.

Post-translational modification

Isoform Cytoplasmic is acetylated at position 2 By similarity. HAMAP-Rule MF_00743

Acetylation of Lys-474 is observed in liver mitochondria from fasted mice but not from fed mice. HAMAP-Rule MF_00743

Miscellaneous

There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors By similarity.

Sequence similarities

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Mitochondrial (identifier: P97807-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Cytoplasmic (identifier: P97807-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: Missing.
Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2 (By similarity).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4141Mitochondrion By similarity
Chain42 – 507466Fumarate hydratase, mitochondrial HAMAP-Rule MF_00743
PRO_0000010323

Regions

Region173 – 1764B site By similarity
Region183 – 1853Substrate binding By similarity

Sites

Binding site1441Substrate By similarity

Amino acid modifications

Modified residue581N6-acetyllysine; alternate Ref.7
Modified residue581N6-succinyllysine; alternate Ref.6
Modified residue631N6-acetyllysine; alternate Ref.6 Ref.7
Modified residue631N6-succinyllysine; alternate Ref.6
Modified residue771N6-acetyllysine; alternate Ref.7
Modified residue771N6-succinyllysine; alternate Ref.6
Modified residue1121N6-acetyllysine; alternate Ref.7
Modified residue1121N6-succinyllysine; alternate Ref.6
Modified residue1191N6-acetyllysine; alternate Ref.7
Modified residue1191N6-succinyllysine; alternate Ref.6
Modified residue2101N6-acetyllysine Ref.7
Modified residue2201N6-acetyllysine; alternate Ref.7
Modified residue2201N6-succinyllysine; alternate Ref.6
Modified residue2891N6-acetyllysine; alternate Ref.7
Modified residue2891N6-succinyllysine; alternate Ref.6
Modified residue4641N6-succinyllysine Ref.6
Modified residue4701N6-succinyllysine Ref.6
Modified residue4991N6-acetyllysine Ref.7

Natural variations

Alternative sequence1 – 4040Missing in isoform Cytoplasmic.
VSP_018967

Experimental info

Sequence conflict1831S → N in AK002379. Ref.1
Sequence conflict2361A → T in AK002379. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Mitochondrial [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 2F24F7B089608ABE

FASTA50754,357
        10         20         30         40         50         60 
MYRALRLLAR SRRLLRVPSA GAAVSGEATT LPRCAPNVAR MASQNSFRVE FDTFGELKVP 

        70         80         90        100        110        120 
TDKYYGAQTV RSTMNFKIGG ATERMPIPVI QAFGILKRAA AEVNQEYGLD PKIASAIMKA 

       130        140        150        160        170        180 
ADEVAEGKLN DHFPLVVWQT GSGTQTNMNV NEVISNRAIE MLGGELGSKK PVHPNDHVNK 

       190        200        210        220        230        240 
SQSSNDTFPT AMHIAAAVEV HKVLLPGLQK LHDALSAKSK EFAQVIKIGR THTQDAVPLT 

       250        260        270        280        290        300 
LGQEFSGYVQ QVQYAMVRIK AAMPRIYELA AGGTAVGTGL NTRIGFAEKV AAKVAALTGL 

       310        320        330        340        350        360 
PFVTAPNKFE ALAAHDALVE LSGAMNTAAC SLMKIANDIR FLGSGPRSGL GELILPENEP 

       370        380        390        400        410        420 
GSSIMPGKVN PTQCEAMTMV AAQVMGNHVA VTVGGSNGHF ELNVFKPMMI KNVLHSARLL 

       430        440        450        460        470        480 
GDASVSFTDN CVVGIQANTE RINKLMNESL MLVTALNPHI GYDKAAKIAK TAHKNGSTLK 

       490        500 
ETAIELGYLT AEQFDEWVKP KDMLGPK 

« Hide

Isoform Cytoplasmic [UniParc].

Checksum: 95ECA9B728E029AF
Show »

FASTA46750,053

References

« Hide 'large scale' references
[1]"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: Heart and Kidney.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
[4]"E2a-Pbx1 induces aberrant expression of tissue-specific and developmentally regulated genes when expressed in NIH 3T3 fibroblasts."
Fu X., Kamps M.P.
Mol. Cell. Biol. 17:1503-1512(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 178-282.
[5]Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 49-71; 85-97; 99-112; 129-157; 181-210; 231-258; 266-283; 294-308; 348-368; 419-441; 445-464 AND 481-501, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-58; LYS-63; LYS-77; LYS-112; LYS-119; LYS-220; LYS-289; LYS-464 AND LYS-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[7]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58; LYS-63; LYS-77; LYS-112; LYS-119; LYS-210; LYS-220; LYS-289 AND LYS-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002379 mRNA. No translation available.
AK147000 mRNA. Translation: BAE27597.1.
CH466555 Genomic DNA. Translation: EDL13210.1.
BC006048 mRNA. Translation: AAH06048.1.
U72679 mRNA. Translation: AAB51039.1.
RefSeqNP_034339.2. NM_010209.2.
UniGeneMm.41502.

3D structure databases

ProteinModelPortalP97807.
SMRP97807. Positions 46-507.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP97807. 6 interactions.
MINTMINT-1859341.

PTM databases

PhosphoSiteP97807.

2D gel databases

REPRODUCTION-2DPAGEIPI00759940.
P97807.

Proteomic databases

PaxDbP97807.
PRIDEP97807.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027810; ENSMUSP00000027810; ENSMUSG00000026526. [P97807-1]
GeneID14194.
KEGGmmu:14194.
UCSCuc007dtn.2. mouse. [P97807-1]

Organism-specific databases

CTD14194.
MGIMGI:95530. Fh1.

Phylogenomic databases

eggNOGCOG0114.
GeneTreeENSGT00390000002779.
HOGENOMHOG000061736.
HOVERGENHBG002183.
InParanoidQ3UIA9.
KOK01679.
OMARIEKDTM.
OrthoDBEOG75J0MX.
TreeFamTF300441.

Enzyme and pathway databases

UniPathwayUPA00223; UER01007.

Gene expression databases

ArrayExpressP97807.
BgeeP97807.
CleanExMM_FH1.
GenevestigatorP97807.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00743. FumaraseC.
InterProIPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERPTHR11444. PTHR11444. 1 hit.
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285416.
PROP97807.
SOURCESearch...

Entry information

Entry nameFUMH_MOUSE
AccessionPrimary (citable) accession number: P97807
Secondary accession number(s): Q3UIA9, Q99JL0, Q9DCX0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 135 of the entry and version 3 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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