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Q9ZCQ4 (FUMC_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:RP665
OrganismRickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.2

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 term3D-structure
Allosteric enzyme
Complete proteome
Reference 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 – 461461Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161307

Regions

Region98 – 1003Substrate binding HAMAP-Rule MF_00743
Region129 – 1324B site By similarity
Region139 – 1413Substrate binding Probable
Region187 – 1882Substrate binding By similarity
Region324 – 3263Substrate binding HAMAP-Rule MF_00743

Sites

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

Secondary structure

............................................................. 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ZCQ4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C9929CC94E7E617D

FASTA46151,008
        10         20         30         40         50         60 
MKNYRIESDS FGEIQIEEKF YWGAQTQRSL NNFKISKQKM PKILIRALAI LKKCAAQVNY 

        70         80         90        100        110        120 
EFGDLEYKIA TSIDKAIDRI LAGEFEDNFP LVVWQTGSGT QTNMNMNEVI ASIANEELTG 

       130        140        150        160        170        180 
KKGGKFPVHP NDHVNKGQSS NDSFPTAMHI ATVLATKQQL IPALNNLLTY LQDKSKDWDK 

       190        200        210        220        230        240 
IIKIGRTHLQ DATPLTLKQE FSGYITQIEY ALERIEDALK KVYLLAQGGT AVGTGINSKI 

       250        260        270        280        290        300 
GFDIKFAQKV AEFTQQPFKT APNKFESLAA HDALVEFSGT LNTIAVSLMK IANDIRLLGS 

       310        320        330        340        350        360 
GPRCGLGELH LPENEPGSSI MPGKVNPTQV EALTMVCTQV MGNHVTVTIA GSNGHLELNV 

       370        380        390        400        410        420 
FKPVIIYNIL QSIELLSDSV NSFVTHCVKG LEPNIARINT LRDKSLMLVT VLNPHIGYDN 

       430        440        450        460 
AAKIAKEAHK YGITLKEAAK KLNFLSEEEF DKIVVPEKMI S 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.
[2]"Structure of fumarate hydratase from Rickettsia prowazekii, the agent of typhus and suspected relative of the mitochondria."
Phan I., Subramanian S., Olsen C., Edwards T.E., Guo W., Zhang Y., Van Voorhis W.C., Stewart L.J., Myler P.J.
Acta Crystallogr. F 67:1123-1128(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ235272 Genomic DNA. Translation: CAA15103.1.
PIRE71672.
RefSeqNP_221027.1. NC_000963.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GTDX-ray2.40A/B1-461[»]
ProteinModelPortalQ9ZCQ4.
SMRQ9ZCQ4. Positions 4-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272947.RP665.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA15103; CAA15103; CAA15103.
GeneID883633.
KEGGrpr:RP665.
PATRIC17902157. VBIRicPro72556_0685.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAMESFNIH.
OrthoDBEOG6V1M4M.

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...

Other

EvolutionaryTraceQ9ZCQ4.

Entry information

Entry nameFUMC_RICPR
AccessionPrimary (citable) accession number: Q9ZCQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: May 1, 1999
Last modified: May 14, 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

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways