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Protein

Fumarate hydratase 1, mitochondrial

Gene

FUM1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

(S)-malate = fumarate + H2O.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei129 – 1291SubstrateBy similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: UniProtKB-EC

GO - Biological processi

  1. fumarate metabolic process Source: InterPro
  2. pollen tube development Source: TAIR
  3. response to oxidative stress Source: TAIR
  4. response to salt stress Source: TAIR
  5. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciARA:GQT-1578-MONOMER.
ReactomeiREACT_242439. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase 1, mitochondrial (EC:4.2.1.2)
Short name:
Fumarase 1
Gene namesi
Name:FUM1
Ordered Locus Names:At2g47510
ORF Names:T30B22.19
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 2

Organism-specific databases

TAIRiAT2G47510.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: TAIR
  2. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionSequence AnalysisAdd
BLAST
Chaini29 – 492464Fumarate hydratase 1, mitochondrialPRO_0000010329Add
BLAST

Proteomic databases

PaxDbiP93033.
PRIDEiP93033.

Expressioni

Gene expression databases

ExpressionAtlasiP93033. baseline.
GenevestigatoriP93033.

Interactioni

Protein-protein interaction databases

BioGridi4699. 1 interaction.
IntActiP93033. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP93033.
SMRiP93033. Positions 31-490.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni157 – 1604B siteBy similarity
Regioni167 – 1693Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
InParanoidiP93033.
KOiK01679.
OMAiMASARRM.
PhylomeDBiP93033.

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]

Sequencei

Sequence statusi: Complete.

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

P93033-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSIYVASRRL SGGTTVTALR YATSLRSYST SFREERDTFG PIQVPSDKLW
60 70 80 90 100
GAQTQRSLQN FEIGGERERM PEPIVRAFGV LKKCAAKVNM EYGLDPTIGK
110 120 130 140 150
AIMQAAQEVA EGKLNDHFPL VVWQTGSGTQ SNMNANEVIA NRAAEILGRK
160 170 180 190 200
RGEKCVHPND HVNRSQSSND TFPTVMHIAA ATEINSRLIP SLKTLHSTLE
210 220 230 240 250
SKSFEFKDIV KIGRTHTQDA TPLTLGQEFG GYATQVKYGL NRVTCTLPRL
260 270 280 290 300
YQLAQGGTAV GTGLNTKKGF DVKIAAAVAE ETNLPFVTAE NKFEALAAHD
310 320 330 340 350
ACVETSGSLN TIATSLMKIA NDIRFLGSGP RCGLGELVLP ENEPGSSIMP
360 370 380 390 400
GKVNPTQCEA LTMVCAQVMG NHVAVTVGGS NGHFELNVFK PVIASALLHS
410 420 430 440 450
VRLIADASAS FEKNCVRGIE ANRERISKLL HESLMLVTSL NPKIGYDNAA
460 470 480 490
AVAKKAHKEG CTLKEAALNL GVLTAEEFDT LVVPEKMIGP SD
Length:492
Mass (Da):53,000
Last modified:December 15, 2003 - v2
Checksum:iDF07D2D393966B3E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 92RR → A in AAB39989. 1 PublicationCurated
Sequence conflicti197 – 1971S → R in AAB39989. 1 PublicationCurated
Sequence conflicti393 – 3942IA → TS in AAB39989. 1 PublicationCurated
Sequence conflicti442 – 4421P → R in AAB39989. 1 PublicationCurated
Sequence conflicti446 – 4461Y → C in AAB39989. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82202 mRNA. Translation: AAB39989.1.
AC002535 Genomic DNA. Translation: AAC62859.1.
CP002685 Genomic DNA. Translation: AEC10852.1.
CP002685 Genomic DNA. Translation: AEC10853.1.
AF020303 Genomic DNA. Translation: AAB71399.1.
AY054252 mRNA. Translation: AAL06911.1.
AY062460 mRNA. Translation: AAL32538.1.
BT003361 mRNA. Translation: AAO29979.1.
PIRiT00433.
RefSeqiNP_001078075.1. NM_001084606.1.
NP_182273.1. NM_130319.3.
UniGeneiAt.10398.

Genome annotation databases

EnsemblPlantsiAT2G47510.1; AT2G47510.1; AT2G47510.
AT2G47510.2; AT2G47510.2; AT2G47510.
GeneIDi819364.
KEGGiath:AT2G47510.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82202 mRNA. Translation: AAB39989.1.
AC002535 Genomic DNA. Translation: AAC62859.1.
CP002685 Genomic DNA. Translation: AEC10852.1.
CP002685 Genomic DNA. Translation: AEC10853.1.
AF020303 Genomic DNA. Translation: AAB71399.1.
AY054252 mRNA. Translation: AAL06911.1.
AY062460 mRNA. Translation: AAL32538.1.
BT003361 mRNA. Translation: AAO29979.1.
PIRiT00433.
RefSeqiNP_001078075.1. NM_001084606.1.
NP_182273.1. NM_130319.3.
UniGeneiAt.10398.

3D structure databases

ProteinModelPortaliP93033.
SMRiP93033. Positions 31-490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4699. 1 interaction.
IntActiP93033. 1 interaction.

Proteomic databases

PaxDbiP93033.
PRIDEiP93033.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G47510.1; AT2G47510.1; AT2G47510.
AT2G47510.2; AT2G47510.2; AT2G47510.
GeneIDi819364.
KEGGiath:AT2G47510.

Organism-specific databases

GeneFarmi4370. 440.
TAIRiAT2G47510.

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
InParanoidiP93033.
KOiK01679.
OMAiMASARRM.
PhylomeDBiP93033.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciARA:GQT-1578-MONOMER.
ReactomeiREACT_242439. Citric acid cycle (TCA cycle).

Gene expression databases

ExpressionAtlasiP93033. baseline.
GenevestigatoriP93033.

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. Behal R.H., Oliver D.J.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
    Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
    Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.

Entry informationi

Entry nameiFUM1_ARATH
AccessioniPrimary (citable) accession number: P93033
Secondary accession number(s): O24649
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: January 7, 2015
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.