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Q8UEY7 (FUMC_AGRT5) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 class II

Short name=Fumarase C
EC=4.2.1.2
Gene names
Name:fumC
Ordered Locus Names:Atu1616
ORF Names:AGR_C_2979
OrganismAgrobacterium tumefaciens (strain C58 / ATCC 33970) [Reference proteome] [HAMAP]
Taxonomic identifier176299 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible addition of water to fumarate to give L-malate By similarity. HAMAP-Rule MF_00743

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

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00743

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00743.

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 processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionfumarate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161251

Regions

Region98 – 1003Substrate binding By similarity
Region129 – 1324B site By similarity
Region139 – 1413Substrate binding By similarity
Region187 – 1882Substrate binding By similarity
Region324 – 3263Substrate binding By similarity

Sites

Active site1881Proton donor/acceptor By similarity
Active site3181 By similarity
Binding site3191Substrate By similarity
Site3311Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8UEY7 [UniParc].

Last modified December 15, 2003. Version 2.
Checksum: CDC3B0A32C5CC41C

FASTA46349,244
        10         20         30         40         50         60 
MTATRTETDT FGPIEVQADR YWGAQAQRSL GNFKIGWEKQ PASVVRALGI VKQAAARANM 

        70         80         90        100        110        120 
ALAGLDPKVG DAIIAAAQEV IDGKLTEHFP LVVWQTGSGT QSNMNANEVI SNRAIEMLGG 

       130        140        150        160        170        180 
EMGTKKPVHP NDHVNMSQSS NDTYPTAMHI ACVEEIVHHL LPALKHLHTA LEAKVKQFEK 

       190        200        210        220        230        240 
IIKIGRTHTQ DATPLTLGQE FSGYAAQVAS AIANIELTLP ALSKLAQGGT AVGTGLNAPV 

       250        260        270        280        290        300 
GFAEKVAEEI SEITGLSFVT APNKFEALAS HDSMVFSHGA INAAAAALFK IANDIRFLGS 

       310        320        330        340        350        360 
GPRAGLGELS LPENEPGSSI MPGKVNPTQS EALTQVCAHI FGNNAALSFA GSQGHFELNV 

       370        380        390        400        410        420 
YNPMMAYNFL QSVQLLGDAA VSFTDNCVVG IEAREDNIRK GVENSLMLVT ALNGKLGYDI 

       430        440        450        460 
CAKIAKTAHK NGTTLREEAV GGGYLTNEEF DQYVRPENMI GPK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE007869 Genomic DNA. Translation: AAK87395.2.
PIRAD2775.
B97555.
RefSeqNP_354610.2. NC_003062.2.

3D structure databases

ProteinModelPortalQ8UEY7.
SMRQ8UEY7. Positions 5-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176299.Atu1616.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK87395; AAK87395; Atu1616.
GeneID1133654.
KEGGatu:Atu1616.
PATRIC20813009. VBIAgrTum91616_1635.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMARIEKDTM.
OrthoDBEOG6V1M4M.
ProtClustDBPRK00485.

Enzyme and pathway databases

UniPathwayUPA00223; UER01007.

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 nameFUMC_AGRT5
AccessionPrimary (citable) accession number: Q8UEY7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: March 19, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways