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P93033 (FUM1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fumarate hydratase 1, mitochondrial

Short name=Fumarase 1
EC=4.2.1.2
Gene names
Name:FUM1
Ordered Locus Names:At2g47510
ORF Names:T30B22.19
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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

Subcellular location

Mitochondrion Ref.5.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Potential
Chain29 – 492464Fumarate hydratase 1, mitochondrial HAMAP-Rule MF_00743
PRO_0000010329

Regions

Region157 – 1604B site By similarity
Region167 – 1693Substrate binding By similarity

Sites

Binding site1291Substrate By similarity

Experimental info

Sequence conflict8 – 92RR → A in AAB39989. Ref.1
Sequence conflict1971S → R in AAB39989. Ref.1
Sequence conflict393 – 3942IA → TS in AAB39989. Ref.1
Sequence conflict4421P → R in AAB39989. Ref.1
Sequence conflict4461Y → C in AAB39989. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P93033 [UniParc].

Last modified December 15, 2003. Version 2.
Checksum: DF07D2D393966B3E

FASTA49253,000
        10         20         30         40         50         60 
MSIYVASRRL SGGTTVTALR YATSLRSYST SFREERDTFG PIQVPSDKLW GAQTQRSLQN 

        70         80         90        100        110        120 
FEIGGERERM PEPIVRAFGV LKKCAAKVNM EYGLDPTIGK AIMQAAQEVA EGKLNDHFPL 

       130        140        150        160        170        180 
VVWQTGSGTQ SNMNANEVIA NRAAEILGRK RGEKCVHPND HVNRSQSSND TFPTVMHIAA 

       190        200        210        220        230        240 
ATEINSRLIP SLKTLHSTLE SKSFEFKDIV KIGRTHTQDA TPLTLGQEFG GYATQVKYGL 

       250        260        270        280        290        300 
NRVTCTLPRL YQLAQGGTAV GTGLNTKKGF DVKIAAAVAE ETNLPFVTAE NKFEALAAHD 

       310        320        330        340        350        360 
ACVETSGSLN TIATSLMKIA NDIRFLGSGP RCGLGELVLP ENEPGSSIMP GKVNPTQCEA 

       370        380        390        400        410        420 
LTMVCAQVMG NHVAVTVGGS NGHFELNVFK PVIASALLHS VRLIADASAS FEKNCVRGIE 

       430        440        450        460        470        480 
ANRERISKLL HESLMLVTSL NPKIGYDNAA AVAKKAHKEG CTLKEAALNL GVLTAEEFDT 

       490 
LVVPEKMIGP SD 

« Hide

References

« Hide 'large scale' references
[1]Behal R.H., Oliver D.J.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT00433.
RefSeqNP_001078075.1. NM_001084606.1.
NP_182273.1. NM_130319.3.
UniGeneAt.10398.

3D structure databases

ProteinModelPortalP93033.
SMRP93033. Positions 31-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid4699. 1 interaction.
IntActP93033. 1 interaction.

Proteomic databases

PaxDbP93033.
PRIDEP93033.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G47510.1; AT2G47510.1; AT2G47510.
AT2G47510.2; AT2G47510.2; AT2G47510.
GeneID819364.
KEGGath:AT2G47510.

Organism-specific databases

GeneFarm4370. 440.
TAIRAT2G47510.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
InParanoidP93033.
KOK01679.
OMASERMPPA.
PhylomeDBP93033.
ProtClustDBPLN00134.

Enzyme and pathway databases

BioCycARA:GQT-1578-MONOMER.
UniPathwayUPA00223; UER01007.

Gene expression databases

GenevestigatorP93033.

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...

Entry information

Entry nameFUM1_ARATH
AccessionPrimary (citable) accession number: P93033
Secondary accession number(s): O24649
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: April 16, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names