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Q83ML8 (FUMC_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 82. 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:SF1634, S1765
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

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_0000161310

Regions

Region98 – 1003Substrate 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
Q83ML8 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 865CBAE31CB2768D

FASTA46750,520
        10         20         30         40         50         60 
MNTVRSEKDS MGAIDVPADK LWGAQTQRSL EHFRISTEKM PTSLIHALAL TKRAAAKVNE 

        70         80         90        100        110        120 
DLDLLSEEKA 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

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005674 Genomic DNA. Translation: AAN43217.1.
AE014073 Genomic DNA. Translation: AAP17104.1.
RefSeqNP_707510.1. NC_004337.2.
NP_837297.1. NC_004741.1.

3D structure databases

ProteinModelPortalQ83ML8.
SMRQ83ML8. Positions 4-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF1634.

Proteomic databases

PaxDbQ83ML8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN43217; AAN43217; SF1634.
AAP17104; AAP17104; S1765.
GeneID1027791.
1078103.
KEGGsfl:SF1634.
sfx:S1765.
PATRIC18704911. VBIShiFle31049_1954.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMARIEKDTM.
OrthoDBEOG6V1M4M.
ProtClustDBPRK00485.

Enzyme and pathway databases

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_SHIFL
AccessionPrimary (citable) accession number: Q83ML8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 82 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

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