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Q9ZJQ9 (FUMC_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 97. 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:jhp_1245
OrganismHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length463 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 – 463463Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161281

Regions

Region97 – 993Substrate binding By similarity
Region128 – 1314B site By similarity
Region138 – 1403Substrate binding By similarity
Region186 – 1872Substrate binding By similarity
Region323 – 3253Substrate binding By similarity

Sites

Active site1871Proton donor/acceptor By similarity
Active site3171 By similarity
Binding site3181Substrate By similarity
Site3301Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZJQ9 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: EF8EEF9CABD1D485

FASTA46350,920
        10         20         30         40         50         60 
MQFRIEHDTM GEIKVDDSQY WGAQTQRSLE NFKIGTEKMP KELIGAFAKL KRSLAVVNHK 

        70         80         90        100        110        120 
LGKLSLEKSQ AIIKACDCIL KGELCGEFPL AIWQTGSGTQ TNMNLNEVIA NKATEILGGN 

       130        140        150        160        170        180 
FREKKLIHPN DDVNMSQSSN DTFPTAMHVV SVLEITHKLL PSLENLLKTF KEKSQQFKEI 

       190        200        210        220        230        240 
VKIGRTHLQD ATPLTLGQEF SGYASMLEHS KQQILESLEH LRELAIGGTA VGTGLNAHKE 

       250        260        270        280        290        300 
LSEKVAEELS QFSGVKFISA PNKFHALTSH DAIAYAHGAF KALAANLMKI ANDIRWLASG 

       310        320        330        340        350        360 
PRCGLGELNI PENEPGSSIM PGKVNPTQCE AMTMVAVQVM GNDTAIGIAA SQGNFELNVF 

       370        380        390        400        410        420 
KPVIIYNFLQ SLRLLSDSME SFNIHCASGI EPNKEKIDYY LHHSLMLVTA LNPHVGYENA 

       430        440        450        460 
AKIAKNAHKK GISLKESALE LKLLSAEDFD QFVVPEKMIG PKA 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99 / ATCC 700824.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001439 Genomic DNA. Translation: AAD06830.1.
PIRH71830.
RefSeqNP_223963.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZJQ9.
SMRQ9ZJQ9. Positions 4-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING85963.jhp1245.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD06830; AAD06830; jhp_1245.
GeneID890413.
KEGGhpj:jhp1245.
PATRIC20607334. VBIHelPyl98156_1348.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
KOK01679.
OMARIEKDTM.
OrthoDBEOG6V1M4M.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycHPYL85963:GJB9-1281-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_HELPJ
AccessionPrimary (citable) accession number: Q9ZJQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: March 19, 2014
This is version 97 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