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Q929E8 (FUMC_LISIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 77. 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:citG
Ordered Locus Names:lin2328
OrganismListeria innocua serovar 6a (strain CLIP 11262) [Complete proteome] [HAMAP]
Taxonomic identifier272626 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length455 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
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 – 455455Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161284

Regions

Region96 – 983Substrate binding By similarity
Region122 – 1254B site By similarity
Region132 – 1343Substrate binding By similarity
Region180 – 1812Substrate binding By similarity
Region317 – 3193Substrate binding By similarity

Sites

Active site1811Proton donor/acceptor By similarity
Active site3111 By similarity
Binding site3121Substrate By similarity
Site3241Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q929E8 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 800F577E7E5BEB38

FASTA45549,737
        10         20         30         40         50         60 
MERIERDTLG EISVDATKYW GAQTERSRRN FAIGDNYMPK EIIYAFAQLK KAAAKVNALE 

        70         80         90        100        110        120 
GKLSEAKSVA IGNVCDQIIQ GELDEHFPLV VWQTGSGTQS NMNVNEVIAH VANLTLGEEK 

       130        140        150        160        170        180 
VHPNDDVNMS QSSNDTFPTA MHIAAYQALV TKLLSEITKM EEVLTTKKNQ YMQLVKIGRT 

       190        200        210        220        230        240 
HLQDATPLTL GQEISGWEAC LTNNKNYLES SMKAILPLAI GGTAVGTGLN ASKDFGDKVA 

       250        260        270        280        290        300 
EELRKQTGYP FTSDSNKYFA LTSHSPINFV HGAIRSLASD LMKIANDIRL LASGPRSGIG 

       310        320        330        340        350        360 
ELTLPANEPG SSIMPGKVNP TQCEAITMVA AQVMGNDTTI NIAASQGNFE LNVYKPVIIF 

       370        380        390        400        410        420 
NFLESITLLS DSMRSFRIHC LEGLTANESV IEAKVNDSLM LVTALNPHIG YEKAAKIAKL 

       430        440        450 
AFDENTTLKE AAIKTGFVTE KEFDLWIDPL KMTNL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL596171 Genomic DNA. Translation: CAC97556.1.
PIRAD1723.
RefSeqNP_471660.1. NC_003212.1.

3D structure databases

ProteinModelPortalQ929E8.
SMRQ929E8. Positions 3-452.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272626.lin2328.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC97556; CAC97556; CAC97556.
GeneID1131082.
KEGGlin:lin2328.
PATRIC20301493. VBILisInn102668_2379.

Organism-specific databases

GenoListLIN2328.
CMRSearch...

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_LISIN
AccessionPrimary (citable) accession number: Q929E8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 1, 2001
Last modified: March 19, 2014
This is version 77 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