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Reviewed, UniProtKB/Swiss-Prot Q9I587 (FUMC2_PSEAE)

Last modified February 9, 2010. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 [Complete proteome] [HAMAP]
Taxonomic identifier287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-malate = fumarate + H2O. HAMAP MF_00743

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP MF_00743

Subunit structure

Homotetramer By similarity. HAMAP MF_00743

Subcellular location

Cytoplasm By similarity HAMAP 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. HAMAP MF_00743

Sequence similarities

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: HAMAP

   Cellular componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionfumarate hydratase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Fumarate hydratase class II 2 HAMAP MF_00743
PRO_0000161300

Regions

Region127 – 1304B site By similarity
Region137 – 1393Substrate binding By similarity

Sites

Binding site981Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9I587-1 [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.

3D structure databases

SMRQ9I587. Positions 3-458.
ModBaseSearch...

Genome annotation databases

GeneID878044.
GenomeReviewsGene locus PA0854 in contig AE004091_GR.
KEGGpae:PA0854.

Organism-specific databases

PseudoCAPPA0854.
CMRSearch...

Phylogenomic databases

HOGENOMHBG284369.
OMAAVCELAQ.

Enzyme and pathway databases

BioCycPAER208964:PA0854-MONOMER.
BRENDA4.2.1.2. 354.

Family and domain databases

HAMAPMF_00743. FumaraseC.
[Tree]
InterProIPR003031. D_crystallin.
IPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
[Graphical view]
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.
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: February 9, 2010
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents