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P93033

- FUM1_ARATH

UniProt

P93033 - FUM1_ARATH

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Protein

Fumarate hydratase 1, mitochondrial

Gene

FUM1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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.
OMAiNAHPEYH.
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 .
PIRi T00433.
RefSeqi NP_001078075.1. NM_001084606.1.
NP_182273.1. NM_130319.3.
UniGenei At.10398.

3D structure databases

ProteinModelPortali P93033.
SMRi P93033. Positions 31-490.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 4699. 1 interaction.
IntActi P93033. 1 interaction.

Proteomic databases

PaxDbi P93033.
PRIDEi P93033.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT2G47510.1 ; AT2G47510.1 ; AT2G47510 .
AT2G47510.2 ; AT2G47510.2 ; AT2G47510 .
GeneIDi 819364.
KEGGi ath:AT2G47510.

Organism-specific databases

GeneFarmi 4370. 440.
TAIRi AT2G47510.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
InParanoidi P93033.
KOi K01679.
OMAi NAHPEYH.
PhylomeDBi P93033.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci ARA:GQT-1578-MONOMER.
Reactomei REACT_242439. Citric acid cycle (TCA cycle).

Gene expression databases

ExpressionAtlasi P93033. baseline.
Genevestigatori P93033.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00743. FumaraseC.
InterProi IPR005677. 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 ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00979. fumC_II. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 116 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