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Q8KTE1 (FUMC_METEA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 65. 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:fumA
Ordered Locus Names:MexAM1_META1p2857
OrganismMethylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1) [Complete proteome] [HAMAP]
Taxonomic identifier272630 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length472 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 – 472472Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161287

Regions

Region105 – 1073Substrate binding By similarity
Region136 – 1394B site By similarity
Region146 – 1483Substrate binding By similarity
Region194 – 1952Substrate binding By similarity
Region331 – 3333Substrate binding By similarity

Sites

Active site1951Proton donor/acceptor By similarity
Active site3251 By similarity
Binding site3261Substrate By similarity
Site3381Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8KTE1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 6B24EDD6A27775E7

FASTA47249,739
        10         20         30         40         50         60 
MSPHENPSVE TRTESDTFGP IEVPAHRYWG AQTQRSIQNF KIGTERQPAP LVHALGIVKQ 

        70         80         90        100        110        120 
AAALVNKDLG GLDPKIADAI AESAAEVVAG KHDDEFPLVV WQTGSGTQSN MNANEVIASL 

       130        140        150        160        170        180 
ANERLGGKRG GKSPVHPNDH CNRGQSSNDT FPTAMHIAVA REVQERLLPA LSHLHTALDA 

       190        200        210        220        230        240 
KAKEFESIVK IGRTHLQDAT PVSLGQEFSG YAAQVALGGA RIAATLPGVL ALAQGGTAVG 

       250        260        270        280        290        300 
TGLNAHPEFA ERFAAKVAEL TGLPFTSAEN KFEALATHDA LVFLQGALTA LASGLFKIAN 

       310        320        330        340        350        360 
DIRLLGSGPR SGLGELSLPE NEPGSSIMPG KVNPTQCEAL TMVCAQVVGN GTTVSFAGSQ 

       370        380        390        400        410        420 
GHFELNVFKP VIANAVLQSV RILADASVSF TDNCVVGIKA NTDRISDLMS RSLMLVTALA 

       430        440        450        460        470 
PSIGYDKAAE IAKTAHKNGT TLKEEALRLG YVTDEEFERV VRPETMLAPS AE 

« Hide

References

« Hide 'large scale' references
[1]"Reconstruction of C3 and C4 metabolism in Methylobacterium extorquens AM1 using transposon mutagenesis."
Van Dien S.J., Okubo Y., Hough M.T., Taitano T., Lidstrom M.E.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Methylobacterium genome sequences: a reference blueprint to investigate microbial metabolism of C1 compounds from natural and industrial sources."
Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E. expand/collapse author list , Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C., Lidstrom M.E.
PLoS ONE 4:E5584-E5584(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14718 / DSM 1338 / AM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF497854 Genomic DNA. Translation: AAN03819.1.
CP001510 Genomic DNA. Translation: ACS40610.1.
RefSeqYP_002963887.1. NC_012808.1.

3D structure databases

ProteinModelPortalQ8KTE1.
SMRQ8KTE1. Positions 12-469.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS40610; ACS40610; MexAM1_META1p2857.
GeneID7992744.
KEGGmea:Mex_1p2857.
PATRIC22511447. VBIMetExt101010_2790.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAIGHHTAI.
OrthoDBEOG6V1M4M.
ProtClustDBCLSK2331283.

Enzyme and pathway databases

BioCycMEXT272630:GBY6-2704-MONOMER.
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_METEA
AccessionPrimary (citable) accession number: Q8KTE1
Secondary accession number(s): C5AUK0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2002
Last modified: March 19, 2014
This is version 65 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