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Reviewed, UniProtKB/Swiss-Prot O84863 (FUMC_CHLTR)

Last modified November 3, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 [Complete proteome] [HAMAP]
Taxonomic identifier813 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-malate = fumarate + H2O. HAMAP MF_00743

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle. HAMAP 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.

Sequence similarities

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termComplete 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 MF_00743
PRO_0000161269

Regions

Region126 – 1294B site By similarity
Region136 – 1383Substrate binding By similarity

Sites

Binding site971Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O84863-1 [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: 9784136] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D/UW-3/Cx.

Cross-references

Sequence databases

AE001273 Genomic DNA. Translation: AAC68452.1.
PIRH71462.
RefSeqNP_220377.1.

3D structure databases

HSSPHSSP built from PDB template 1FUR based on UniProtKB P05042.
ModBaseSearch...

2-D gel databases

PHCI-2DPAGEO84863.

Genome annotation databases

GeneID884656.
GenomeReviewsGene locus CT_855 in contig AE001273_GR.
KEGGctr:CT855.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO84863.
OMAGSQGHFE.

Enzyme and pathway databases

BioCycCTRA315277:CT855-MON.
BRENDA4.2.1.2. 108.

Family and domain databases

HAMAPMF_00743.
[Tree]
InterProIPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
[Graphical view]
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
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: November 3, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents