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Protein

Fumarate hydratase, mitochondrial

Gene

Fh

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

Functioni

Catalytic activityi

(S)-malate = fumarate + H2O.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei144 – 1441SubstrateBy similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: MGI

GO - Biological processi

  1. fumarate metabolic process Source: InterPro
  2. homeostasis of number of cells within a tissue Source: MGI
  3. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiREACT_249033. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase, mitochondrial (EC:4.2.1.2)
Short name:
Fumarase
Alternative name(s):
EF-3
Gene namesi
Name:Fh
Synonyms:Fh1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:95530. Fh1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. mitochondrion Source: MGI
  3. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4141MitochondrionBy similarityAdd
BLAST
Chaini42 – 507466Fumarate hydratase, mitochondrialPRO_0000010323Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581N6-acetyllysine; alternate1 Publication
Modified residuei58 – 581N6-succinyllysine; alternate1 Publication
Modified residuei63 – 631N6-acetyllysine; alternate2 Publications
Modified residuei63 – 631N6-succinyllysine; alternate1 Publication
Modified residuei77 – 771N6-acetyllysine; alternate1 Publication
Modified residuei77 – 771N6-succinyllysine; alternate1 Publication
Modified residuei112 – 1121N6-acetyllysine; alternate1 Publication
Modified residuei112 – 1121N6-succinyllysine; alternate1 Publication
Modified residuei119 – 1191N6-acetyllysine; alternate1 Publication
Modified residuei119 – 1191N6-succinyllysine; alternate1 Publication
Modified residuei210 – 2101N6-acetyllysine1 Publication
Modified residuei220 – 2201N6-acetyllysine; alternate1 Publication
Modified residuei220 – 2201N6-succinyllysine; alternate1 Publication
Modified residuei289 – 2891N6-acetyllysine; alternate1 Publication
Modified residuei289 – 2891N6-succinyllysine; alternate1 Publication
Modified residuei464 – 4641N6-succinyllysine1 Publication
Modified residuei470 – 4701N6-succinyllysine1 Publication
Modified residuei499 – 4991N6-acetyllysine1 Publication

Post-translational modificationi

Isoform Cytoplasmic is acetylated at position 2.By similarity
Acetylation of Lys-474 is observed in liver mitochondria from fasted mice but not from fed mice.2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP97807.
PaxDbiP97807.
PRIDEiP97807.

2D gel databases

REPRODUCTION-2DPAGEIPI00759940.
P97807.

PTM databases

PhosphoSiteiP97807.

Expressioni

Gene expression databases

BgeeiP97807.
CleanExiMM_FH1.
ExpressionAtlasiP97807. baseline and differential.
GenevestigatoriP97807.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi199665. 1 interaction.
IntActiP97807. 6 interactions.
MINTiMINT-1859341.

Structurei

3D structure databases

ProteinModelPortaliP97807.
SMRiP97807. Positions 46-507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 1764B siteBy similarity
Regioni183 – 1853Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0114.
GeneTreeiENSGT00390000002779.
HOGENOMiHOG000061736.
HOVERGENiHBG002183.
InParanoidiP97807.
KOiK01679.
OMAiNTPKGYD.
OrthoDBiEOG75J0MX.
TreeFamiTF300441.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. 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]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform Mitochondrial (identifier: P97807-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MYRALRLLAR SRRLLRVPSA GAAVSGEATT LPRCAPNVAR MASQNSFRVE
60 70 80 90 100
FDTFGELKVP TDKYYGAQTV RSTMNFKIGG ATERMPIPVI QAFGILKRAA
110 120 130 140 150
AEVNQEYGLD PKIASAIMKA ADEVAEGKLN DHFPLVVWQT GSGTQTNMNV
160 170 180 190 200
NEVISNRAIE MLGGELGSKK PVHPNDHVNK SQSSNDTFPT AMHIAAAVEV
210 220 230 240 250
HKVLLPGLQK LHDALSAKSK EFAQVIKIGR THTQDAVPLT LGQEFSGYVQ
260 270 280 290 300
QVQYAMVRIK AAMPRIYELA AGGTAVGTGL NTRIGFAEKV AAKVAALTGL
310 320 330 340 350
PFVTAPNKFE ALAAHDALVE LSGAMNTAAC SLMKIANDIR FLGSGPRSGL
360 370 380 390 400
GELILPENEP GSSIMPGKVN PTQCEAMTMV AAQVMGNHVA VTVGGSNGHF
410 420 430 440 450
ELNVFKPMMI KNVLHSARLL GDASVSFTDN CVVGIQANTE RINKLMNESL
460 470 480 490 500
MLVTALNPHI GYDKAAKIAK TAHKNGSTLK ETAIELGYLT AEQFDEWVKP

KDMLGPK
Length:507
Mass (Da):54,357
Last modified:July 27, 2011 - v3
Checksum:i2F24F7B089608ABE
GO
Isoform Cytoplasmic (identifier: P97807-2) [UniParc]FASTAAdd to Basket

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).By similarity

Show »
Length:467
Mass (Da):50,053
Checksum:i95ECA9B728E029AF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1831S → N in AK002379. (PubMed:16141072)Curated
Sequence conflicti236 – 2361A → T in AK002379. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4040Missing in isoform Cytoplasmic. CuratedVSP_018967Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15547.1. [P97807-1]
RefSeqiNP_034339.2. NM_010209.2. [P97807-1]
UniGeneiMm.41502.

Genome annotation databases

EnsembliENSMUST00000027810; ENSMUSP00000027810; ENSMUSG00000026526. [P97807-1]
GeneIDi14194.
KEGGimmu:14194.
UCSCiuc007dtn.2. mouse. [P97807-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15547.1. [P97807-1]
RefSeqiNP_034339.2. NM_010209.2. [P97807-1]
UniGeneiMm.41502.

3D structure databases

ProteinModelPortaliP97807.
SMRiP97807. Positions 46-507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199665. 1 interaction.
IntActiP97807. 6 interactions.
MINTiMINT-1859341.

PTM databases

PhosphoSiteiP97807.

2D gel databases

REPRODUCTION-2DPAGEIPI00759940.
P97807.

Proteomic databases

MaxQBiP97807.
PaxDbiP97807.
PRIDEiP97807.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027810; ENSMUSP00000027810; ENSMUSG00000026526. [P97807-1]
GeneIDi14194.
KEGGimmu:14194.
UCSCiuc007dtn.2. mouse. [P97807-1]

Organism-specific databases

CTDi14194.
MGIiMGI:95530. Fh1.

Phylogenomic databases

eggNOGiCOG0114.
GeneTreeiENSGT00390000002779.
HOGENOMiHOG000061736.
HOVERGENiHBG002183.
InParanoidiP97807.
KOiK01679.
OMAiNTPKGYD.
OrthoDBiEOG75J0MX.
TreeFamiTF300441.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
ReactomeiREACT_249033. Citric acid cycle (TCA cycle).

Miscellaneous databases

NextBioi285416.
PROiP97807.
SOURCEiSearch...

Gene expression databases

BgeeiP97807.
CleanExiMM_FH1.
ExpressionAtlasiP97807. baseline and differential.
GenevestigatoriP97807.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. 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]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiFUMH_MOUSE
AccessioniPrimary (citable) accession number: P97807
Secondary accession number(s): Q3UIA9, Q99JL0, Q9DCX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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).By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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. 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.