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Q82ID7 (FUMC_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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
Ordered Locus Names:SAV_3221
OrganismStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP]
Taxonomic identifier227882 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length467 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 – 467467Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161321

Regions

Region104 – 1063Substrate binding By similarity
Region129 – 1324B site By similarity
Region139 – 1413Substrate binding By similarity
Region187 – 1882Substrate binding By similarity
Region324 – 3263Substrate binding By similarity

Sites

Active site1881Proton donor/acceptor By similarity
Active site3181 By similarity
Binding site3191Substrate By similarity
Site3311Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82ID7 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 5D984D1060B87F36

FASTA46749,801
        10         20         30         40         50         60 
MTDEDDKQNY RVEHDSMGEV RVPADAKWRA QTQRAVENFP ISGQRLERAH IEALARIKGA 

        70         80         90        100        110        120 
AAKVNAELGV LDKDVAEAIQ EAAAEVAEGR WDEHFPVDVF QTGSGTSSNM NANEVIATLA 

       130        140        150        160        170        180 
TERLGRDVHP NDHVNASQSS NDVFPSSIHI AATAAVTRDL VPALEHLAAA LGRKSEEFAD 

       190        200        210        220        230        240 
VVKAGRTHLM DATPVTLGQE FGGYAAQVRY GVERLAASLP RLAELPLGGT AVGTGINTPP 

       250        260        270        280        290        300 
GFSAAVIAEV ARVTGLPLTE ARDHFEAQGA RDGIVETSGQ LRTIAVGLTK IANDLRWMAS 

       310        320        330        340        350        360 
GPRTGLSEIS LPDLQPGSSI MPGKVNPVIP EAVLMVAAQV TGNDATVAAA GAAGNFELNV 

       370        380        390        400        410        420 
MLPVIAKNVL ESVRLLAHVS RLLADRTVDG IVAHRDRARE YAESSPSVVT PLNKYIGYEE 

       430        440        450        460 
AAKVAKKALA ERQTIRQVVL ESGYVDRGDL TLEQLDEALD VLRMTHP 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000030 Genomic DNA. Translation: BAC70932.1.
RefSeqNP_824397.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ82ID7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227882.SAV_3221.

Proteomic databases

PRIDEQ82ID7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC70932; BAC70932; SAV_3221.
GeneID1210693.
KEGGsma:SAV_3221.
PATRIC23720069. VBIStrAve112782_3441.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061737.
KOK01679.
OMAHANQMAS.
OrthoDBEOG6V1M4M.

Enzyme and pathway databases

BioCycSAVE227882:GJU1-3245-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.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_STRAW
AccessionPrimary (citable) accession number: Q82ID7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 76 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