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Q9I587 (FUMC2_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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 2

Short name=Fumarase C 2
EC=4.2.1.2
Gene names
Name:fumC2
Ordered Locus Names:PA0854
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length464 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 – 464464Fumarate hydratase class II 2 HAMAP-Rule MF_00743
PRO_0000161300

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
Q9I587 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: B0520F835C0DDF61

FASTA46449,122
        10         20         30         40         50         60 
MSRTETDSLG TIEVPDDAYW GAQTQRSLEN FAIGGQRMPL AVIHALALIK KAAARVNDHL 

        70         80         90        100        110        120 
GELPPEVARL IEQAADEVLA GRHDEHFPLV VWQTGSGTQT NMNVNEVIAG RANELAGNPR 

       130        140        150        160        170        180 
GGKSPVHPND HVNRAQSSND SFPTAMHIAA AKAVHEQLLP AIAELSGGLA EQSARHASLV 

       190        200        210        220        230        240 
KTGRTHLMDA TPITFGQELS AFVAQLDYAE RAIRAALPAV YQLAQGGTAV GTGLNAPKGF 

       250        260        270        280        290        300 
ADAIAAEIAA ESGLPFVAAP NKFAALAGHE PLVILSGALK SLAVALMKIA NDLRLLGSGP 

       310        320        330        340        350        360 
RAGFAEVKLP ANEPGSSIMP GKVNPTQCEA LSMLACQVMG NDSTISFAAS QGHLQLNVFK 

       370        380        390        400        410        420 
PVIVYNLLES IRLLADGCRN FNKHCVAGLE PDAQRMADLL ERGLMLVTAL NPHIGYDKAA 

       430        440        450        460 
EIAKKAYAEG TTLRAAALQL GYLDEAQFDE WVRPEQMLEA GHHG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG04243.1.
PIRH83538.
RefSeqNP_249545.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9I587.
SMRQ9I587. Positions 3-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA0854.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID878044.
KEGGpae:PA0854.
PATRIC19835988. VBIPseAer58763_0886.

Organism-specific databases

PseudoCAPPA0854.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAGLNMNIN.
OrthoDBEOG6V1M4M.
ProtClustDBPRK12425.

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 nameFUMC2_PSEAE
AccessionPrimary (citable) accession number: Q9I587
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 82 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