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O84863 (FUMC_CHLTR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:CT_855
OrganismChlamydia trachomatis (strain D/UW-3/Cx) [Reference proteome] [HAMAP]
Taxonomic identifier272561 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia ›

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.

Subcellular location

Cytoplasm By similarity.

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-Rule 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 termAllosteric 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: HAMAP

   Cellular_componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionfumarate hydratase activity

Inferred from electronic annotation. Source: 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_0000161269

Regions

Region95 – 973Substrate binding By similarity
Region126 – 1294B site By similarity
Region136 – 1383Substrate binding By similarity
Region184 – 1852Substrate binding By similarity
Region321 – 3233Substrate binding By similarity

Sites

Active site1851Proton donor/acceptor By similarity
Active site3151 By similarity
Binding site3161Substrate By similarity
Site3281Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
O84863 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 428E3DA10A839853

FASTA46350,339
        10         20         30         40         50         60 
MRQENDSLGI VLVPEDKLFG AQTGRSQEFF SYGKESMPLE IIHALVKIKK CAAKANGDLG 

        70         80         90        100        110        120 
CLDAKRRDMI VAATDEILSG EFDEHFPLKV WQTGSGTQSN MNVNEVIANL AIQRHGGELG 

       130        140        150        160        170        180 
SKHPVHPNDH VNKSQSSNDV FPTAMHIAAV QSIKGSLIPA LEHLKKVIDA KALEFARDIK 

       190        200        210        220        230        240 
IGRTHLMDAV PMTLGQEFSG YSCQLHNCLE RIGFSLTHLY ELAIGGTAIG TGLNVPEGFV 

       250        260        270        280        290        300 
EKVIQYLRRE TGEPFVPASN YFAALSNHDA LVQAHGSLTV LACALVKIAT DLSFLGSGPR 

       310        320        330        340        350        360 
CGLGEIFFPE NEPGSSIMPG KINPTQSEAL QMVCSQVIGN NQSIIFSGTK GNFELNVMKP 

       370        380        390        400        410        420 
VIIYDFLQSV NLLAGAMRSF ADYFVCGLKV NKGQLQQNVE RSLMLVTALA PVLGYDKCSK 

       430        440        450        460 
IALKAFHENL SLKEACVSLG FLSEKEFDEH VIPGLMVGNR GHE

« Hide

References

[1]"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis."
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.
Science 282:754-759(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D/UW-3/Cx.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE001273 Genomic DNA. Translation: AAC68452.1.
PIRH71462.
RefSeqNP_220377.1. NC_000117.1.

3D structure databases

ProteinModelPortalO84863.
SMRO84863. Positions 1-456.
ModBaseSearch...

Protein-protein interaction databases

STRING272561.CT855.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC68452; AAC68452; CT_855.
GeneID884656.
KEGGctr:CT855.
PATRIC20381432. VBIChlTra43535_0944.

Phylogenomic databases

eggNOGCOG0114.
KOK01679.
OMAKDTMGEV.
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.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
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_CHLTR
AccessionPrimary (citable) accession number: O84863
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: November 1, 1998
Last modified: May 1, 2013
This is version 78 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

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