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Q885V0 (FUMC_PSESM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fumarate hydratase class II

Short name=Fumarase C
EC=4.2.1.2
Gene names
Name: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)

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: UniProtKB-KW

   Cellular componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionfumarate hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Fumarate hydratase class II HAMAP MF_00743
PRO_0000161302

Regions

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

Sites

Binding site981Substrate 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...

2D gel databases

World-2DPAGE0008:Q885V0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1183368.
GenomeReviewsGene locus PSPTO_1731 in contig AE016853_GR.
KEGGpst:PSPTO_1731.
NMPDRfig|223283.1.peg.1694.
PATRIC19994714. VBIPseSyr93040_1758.
TIGRPSPTO_1731.

Phylogenomic databases

HOGENOMHBG284369.
OMAAGHEPLT.
ProtClustDBPRK12425.

Enzyme and pathway databases

BioCycPSYR223283:PSPTO_1731-MONOMER.

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.
IPR024083. L-Aspartase-like_N.
IPR022761. Lyase1_N.
[Graphical view]
Gene3DG3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.
KOK01679.
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.
SUPFAMSSF48557. L-Aspartase-like. 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: January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families