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P0AC34 (FUMA_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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 I, aerobic

Short name=Fumarase
EC=4.2.1.2
Gene names
Name:fumA
Ordered Locus Names:c2004
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

It functions as an aerobic enzyme in the citric acid cycle. It accounts for about 80% of the fumarase activity when the bacteria grows aerobically By similarity.

Catalytic activity

(S)-malate = fumarate + H2O.

Cofactor

Binds 1 4Fe-4S cluster By similarity.

Enzyme regulation

Subject to aerobic respiratory control and catabolite repression.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the class-I fumarase family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

fumarate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 548547Fumarate hydratase class I, aerobic
PRO_0000195658

Sites

Active site3971 Potential
Metal binding3181Iron-sulfur (4Fe-4S) By similarity
Binding site4631Substrate Potential

Sequences

Sequence LengthMass (Da)Tools
P0AC34 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6082744088C64603

FASTA54860,299
        10         20         30         40         50         60 
MSNKPFHYQA PFPLKKDDTE YYLLTSEHVS VSEFEGQEIL KVAPEALTLL ARQAFHDASF 

        70         80         90        100        110        120 
MLRPAHQQQV ADILRDPEAS ENDKYVALQF LRNSDIAAKG VLPTCQDTGT AIIVGKKGQR 

       130        140        150        160        170        180 
VWTGGGDEAA LARGVYNTYI EDNLRYSQNA PLDMYKEVNT GTNLPAQIDL YAVDGDEYKF 

       190        200        210        220        230        240 
LCIAKGGGSA NKTYLYQETK ALLTPGKLKN YLVEKMRTLG TAACPPYHIA FVIGGTSAET 

       250        260        270        280        290        300 
NLKTVKLASA KYYDELPTEG NEHGQAFRDV ELEKELLIEA QNLGLGAQFG GKYFAHDIRV 

       310        320        330        340        350        360 
IRLPRHGASC PVGMGVSCSA DRNIKAKINR QGIWIEKLEH NPGKYIPEEL RKAGEGEAVR 

       370        380        390        400        410        420 
VDLNRPMKEI LAQLSQYPVS TRLSLNGTII VGRDIAHAKL KERMDNGEGL PQYIKDHPIY 

       430        440        450        460        470        480 
YAGPAKTPEG YASGSLGPTT AGRMDSYVDQ LQAQGGSMIM LAKGNRSQQV TDACKKHGGF 

       490        500        510        520        530        540 
YLGSIGGPAA VLAQGSIKSL ECVEYPELGM EAIWKIEVED FPAFILVDDK GNDFFQQIQL 


TQCTRCVK 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN80464.1.
RefSeqNP_753899.1. NC_004431.1.

3D structure databases

ProteinModelPortalP0AC34.
SMRP0AC34. Positions 356-537.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c2004.

Proteomic databases

PRIDEP0AC34.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN80464; AAN80464; c2004.
GeneID1036044.
KEGGecc:c2004.
PATRIC18281905. VBIEscCol75197_1871.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000009338.
KOK01676.
OMATCVEYPE.
OrthoDBEOG6TXR10.

Enzyme and pathway databases

BioCycECOL199310:C2004-MONOMER.
UniPathwayUPA00223; UER01007.

Family and domain databases

Gene3D3.20.130.10. 1 hit.
InterProIPR004646. Fe-S_hydro-lyase_TtdA-typ_cat.
IPR004647. Fe-S_hydro-lyase_TtdB-typ_cat.
IPR011167. Fe_dep_fumarate_hydratase.
IPR020557. Fumarate_lyase_CS.
[Graphical view]
PfamPF05681. Fumerase. 1 hit.
PF05683. Fumerase_C. 1 hit.
[Graphical view]
PIRSFPIRSF001394. Fe_dep_fumar_hy. 1 hit.
SUPFAMSSF117457. SSF117457. 1 hit.
TIGRFAMsTIGR00722. ttdA_fumA_fumB. 1 hit.
TIGR00723. ttdB_fumA_fumB. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMA_ECOL6
AccessionPrimary (citable) accession number: P0AC34
Secondary accession number(s): P00923, P76889
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 62 of the entry and version 2 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