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Reviewed, UniProtKB/Swiss-Prot Q929E8 (FUMC_LISIN)

Last modified November 3, 2009. Version 46. 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
      Short name=Fumarase C
    EC=4.2.1.2
Gene names
Name: fumC
Synonyms: citG
Ordered Locus Names: lin2328
OrganismListeria innocua [Complete proteome] [HAMAP]
Taxonomic identifier1642 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesListeriaceaeListeria

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle. HAMAP MF_00743

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

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 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 – 455455Fumarate hydratase class II HAMAP MF_00743
PRO_0000161284

Regions

Region122 – 1254B site By similarity
Region132 – 1343Substrate binding By similarity

Sites

Binding site981Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q929E8-1 [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

AL596171 Genomic DNA. Translation: CAC97556.1.
PIRAD1723.
RefSeqNP_471660.1.

3D structure databases

HSSPHSSP built from PDB template 1FUR based on UniProtKB P05042.
ModBaseSearch...

Genome annotation databases

GeneID1131082.
GenomeReviewsGene locus lin2328 in contig AL592022_GR.
KEGGlin:lin2328.
NMPDRfig|272626.1.peg.2313.

Organism-specific databases

ListiListLIN02328.
CMRSearch...

Phylogenomic databases

HOGENOMQ929E8.
OMAGSQGHFE.

Enzyme and pathway databases

BioCycLINN272626:LIN2328-MON.
BRENDA4.2.1.2. 270396.

Family and domain databases

HAMAPMF_00743.
[Tree]
InterProIPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
[Graphical view]
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
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: November 3, 2009
This is version 46 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