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Q885V0 (FUMC_PSESM) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. 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
Synonyms:fumC-1
Ordered Locus Names:PSPTO_1731
OrganismPseudomonas syringae pv. tomato (strain DC3000) [Complete proteome] [HAMAP]
Taxonomic identifier223283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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
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 – 464464Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161302

Regions

Region96 – 983Substrate binding By similarity
Region127 – 1304B site By similarity
Region137 – 1393Substrate binding By similarity
Region185 – 1862Substrate binding By similarity
Region322 – 3243Substrate binding By similarity

Sites

Active site1861Proton donor/acceptor By similarity
Active site3161 By similarity
Binding site3171Substrate By similarity
Site3291Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q885V0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 6B12FFF27257FFD2

FASTA46449,077
        10         20         30         40         50         60 
MSRTETDSIG PIEVPEDAYW GAQTQRSLIN FAIGDQRMPL AVLHALTLIK KAAARVNDRN 

        70         80         90        100        110        120 
GDLPADIARL IEQAADEVLD GQHDAQFPLV VWQTGSGTQS NMNVNEVIAG RANELAGQGR 

       130        140        150        160        170        180 
GGKSPVHPND HVNRSQSSND CFPTAMHIAT AQAVKEQLLP AIAELSSGLA EQAARHMKLV 

       190        200        210        220        230        240 
KTGRTHMMDA TPITFGQELS GFVAQLDYAE KAIRAALPAV YELAQGGTAV GTGLNAPKGF 

       250        260        270        280        290        300 
AEAIAAELAA LSGLPFVTAP NKFAALAGHE PLAALSGALK TLAGTLMKIA NDLRLLGSGP 

       310        320        330        340        350        360 
RAGLAEVRLP ANEPGSSIMP GKVNPTQCEA LSMLACQVMG NDVTIGFAAS QGHLQLNVYK 

       370        380        390        400        410        420 
PVIIHNVLQS IRLLADGCSN FNEHCVAGME PDAEKMAEHL ERGLMLVTAL NPHIGYDKSA 

       430        440        450        460 
HIAKKAYTEG LTLREAALAL GYLTDEEFDA WVRPDKMLEA GSNG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016853 Genomic DNA. Translation: AAO55251.1.
RefSeqNP_791556.1. NC_004578.1.

3D structure databases

ProteinModelPortalQ885V0.
SMRQ885V0. Positions 3-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223283.PSPTO_1731.

2D gel databases

World-2DPAGE0008:Q885V0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO55251; AAO55251; PSPTO_1731.
GeneID1183368.
KEGGpst:PSPTO_1731.
PATRIC19994714. VBIPseSyr93040_1758.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAAARHMKL.
OrthoDBEOG6V1M4M.
PhylomeDBQ885V0.

Enzyme and pathway databases

BioCycPSYR223283:GJIX-1762-MONOMER.
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_PSESM
AccessionPrimary (citable) accession number: Q885V0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 81 of the entry and version 1 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