Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8X769 (FUMC_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. 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
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:Z2614, ECs2317
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 – 467467Fumarate hydratase class II HAMAP MF_00743
PRO_0000161276

Regions

Region129 – 1324B site By similarity
Region139 – 1413Substrate binding By similarity

Sites

Binding site1001Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8X769 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 6A4F47D2FC0E343F

FASTA46750,462
        10         20         30         40         50         60 
MNTVRSEKDS MGAIDVPADK LWGAQTQRSL EHFRISTEKM PTSLIHALAL TKRAAAKVNE 

        70         80         90        100        110        120 
DLGLLSEEKA SAIRQAADEV LAGQHDDEFP LAIWQTGSGT QSNMNMNEVL ANRASELLGG 

       130        140        150        160        170        180 
VRGMERKVHP NDDVNKSQSS NDVFPTAMHV AALLALRKQL IPQLKTLTQT LSEKSRAFAD 

       190        200        210        220        230        240 
IVKIGRTHLQ DATPLTLGQE ISGWVAMLEH NLKHIEYSLP HVAELALGGT AVGTGLNTHP 

       250        260        270        280        290        300 
EYARRVADEL AVITCAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS 

       310        320        330        340        350        360 
GPRCGIGEIS IPENEPGSSI MPGKVNPTQC EALTMLCCQV MGNDVAINMG GASGNFELNV 

       370        380        390        400        410        420 
FRPMVIHNFL QSVRLLADGM ESFNKHCAVG IEPNRERINQ LLNESLMLVT ALNTHIGYDK 

       430        440        450        460 
AAEIAKKAHK EGLTLKAAAL ALGYLSEAEF DSWVRPEQMV GSMKAGR

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005174 Genomic DNA. Translation: AAG56598.1.
BA000007 Genomic DNA. Translation: BAB35740.1.
PIRB85767.
E90918.
RefSeqNP_288046.1. NC_002655.2.
NP_310344.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8X769.
SMRQ8X769. Positions 4-459.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000027538; EBESCP00000026431; EBESCG00000026590.
EBESCT00000056789; EBESCP00000054617; EBESCG00000055837.
GeneID913708.
961561.
GenomeReviewsGene locus Z2614 in contig AE005174_GR.
Gene locus ECs2317 in contig BA000007_GR.
KEGGece:Z2614.
ecs:ECs2317.
PATRIC18353962. VBIEscCol44059_2194.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000008403.
HOGENOMHBG284369.
OMARIEKDTM.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycECOL83334:ECS2317-MONOMER.

Family and domain databases

HAMAPMF_00743. FumaraseC.
[Tree]
InterProIPR005677. 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]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. L-Aspartase-like. 1 hit.
TIGRFAMsTIGR00979. FumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_ECO57
AccessionPrimary (citable) accession number: Q8X769
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2002
Last modified: January 25, 2012
This is version 64 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents