Fumarate hydratase 1, mitochondrial precursor - Arabidopsis thaliana (Mouse-ear cress)

Contribute

Send feedback

Read comments (?) or add your own

P93033 (FUM1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	492 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(S)-malate = fumarate + H₂O.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subcellular location	Mitochondrion.
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.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fumarate metabolic process Inferred from electronic annotation. Source: InterPro pollen tube development Inferred from mutant phenotype PubMed 19237690. Source: TAIR response to oxidative stress Inferred from direct assay PubMed 12492832. Source: TAIR response to salt stress Inferred from expression pattern PubMed 17916636. Source: TAIR tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrion Inferred from direct assay PubMed 11743115 PubMed 12492832 Ref.5 PubMed 18385124 PubMed 22923678. Source: TAIR tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro
Molecular_function	fumarate hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 28

Mitochondrion Potential

Chain

29 – 492

464

Fumarate hydratase 1, mitochondrial

PRO_0000010329

Regions

Region

157 – 160

B site By similarity

Region

167 – 169

Substrate binding By similarity

Sites

Binding site

129

Substrate By similarity

Experimental info

Sequence conflict

8 – 9

RR → A in AAB39989. Ref.1

Sequence conflict

197

S → R in AAB39989. Ref.1

Sequence conflict

393 – 394

IA → TS in AAB39989. Ref.1

Sequence conflict

442

P → R in AAB39989. Ref.1

Sequence conflict

446

Y → C in AAB39989. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P93033 [UniParc].

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

FASTA

492

53,000

        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' referencesShow '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. 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. 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Strain: cv. Landsberg erecta.
+	Additional computationally mapped references.

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.
IPI	IPI00520007.
PIR	T00433.
RefSeq	NP_001078075.1. NM_001084606.1. NP_182273.1. NM_130319.3.
UniGene	At.10398.
3D structure databases
ProteinModelPortal	P93033.
SMR	P93033. Positions 31-490.
ModBase	Search...
Protein-protein interaction databases
IntAct	P93033. 1 interaction.
Proteomic databases
PaxDb	P93033.
PRIDE	P93033.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G47510.1; AT2G47510.1; AT2G47510. AT2G47510.2; AT2G47510.2; AT2G47510.
GeneID	819364.
KEGG	ath:AT2G47510.
Organism-specific databases
GeneFarm	4370. 440.
TAIR	At2g47510.
Phylogenomic databases
eggNOG	COG0114.
HOGENOM	HOG000061736.
InParanoid	P93033.
KO	K01679.
OMA	KTGRTHM.
PhylomeDB	P93033.
ProtClustDB	PLN00134.
Enzyme and pathway databases
UniPathway	UPA00223; UER01007.
Gene expression databases
ArrayExpress	P93033.
Genevestigator	P93033.
GermOnline	AT2G47510. Arabidopsis thaliana.
Family and domain databases
Gene3D	1.10.275.10. 1 hit.
InterPro	IPR005677. Fum_hydII. IPR024083. Fumarase/histidase_N. IPR018951. Fumarase_C_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR022761. Fumarate_lyase_N. IPR008948. L-Aspartase-like. [Graphical view]
Pfam	PF10415. FumaraseC_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00149. FUMRATELYASE.
SUPFAM	SSF48557. L-Aspartase-like. 1 hit.
TIGRFAMs	TIGR00979. fumC_II. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUM1_ARATH

Accession

Primary (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:	May 1, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents