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Reviewed, UniProtKB/Swiss-Prot Q822D5 (FUMC_CHLCV)

Last modified November 3, 2009. Version 42. 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: CCA_00748
OrganismChlamydophila caviae [Complete proteome] [HAMAP]
Taxonomic identifier83557 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydophila

Protein attributes

Sequence length460 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 – 460460Fumarate hydratase class II HAMAP MF_00743
PRO_0000161266

Regions

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

Sites

Binding site971Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q822D5-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 8F68DE2F0046AFDA

FASTA46050,259
        10         20         30         40         50         60 
MRQENDSLGI VEVPEDKLYG AQTARSQKYF SWAPEVMPKE VIRALVLIKQ CAAKANHDLG 

        70         80         90        100        110        120 
FLDSKYCDMI VSAASEILEG GFEEHFPLKV WQTGSGTQSN MNVNEVIANL AIQRHGGVVG 

       130        140        150        160        170        180 
SKTPIHPNDH VNKSQSSNDV FPTAMHIAAV INLKKKLIPA MDHLQRALDA KVAEFRDCVK 

       190        200        210        220        230        240 
IGRTHLMDAV PMTLGQEFSG YSNQIRQSLE RVAFSLTHMY ELAIGGTAVG TGLNVPNGFI 

       250        260        270        280        290        300 
DKVIHYLRQE TGEPFVAASN YFSALSNHDT LVNAHGVLAT LACALTKIAT DLSFLGSGPR 

       310        320        330        340        350        360 
CGLGELLFPE NEPGSSIMPG KINPTQCEAL QMVCAQVIGN NQAVIMGGSR GNFELNVMKP 

       370        380        390        400        410        420 
VIIYNFLQSV DILAGGMQAF ADYFVSGLRV NKPRLKEYLD NSLMLVTALT PVLGYDKCSK 

       430        440        450        460 
MALKAFHDNI NLKEACIQMG YLSAEEFDRL VVPESMVGKF 

« Hide

References

[1]"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G. expand/collapse author list , Rank R.G., Bavoil P.M., Fraser C.M.
Nucleic Acids Res. 31:2134-2147(2003) [PubMed: 12682364] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GPIC.

Cross-references

Sequence databases

AE015925 Genomic DNA. Translation: AAP05489.1.
RefSeqNP_829611.1.

3D structure databases

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

Genome annotation databases

GeneID1218433.
GenomeReviewsGene locus CCA_00748 in contig AE015925_GR.
KEGGcca:CCA00748.
TIGRCCA_00748.

Phylogenomic databases

HOGENOMQ822D5.
OMAGSQGHFE.

Enzyme and pathway databases

BioCycCCAV227941:CCA_00748-MON.
BRENDA4.2.1.2. 304519.

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_CHLCV
AccessionPrimary (citable) accession number: Q822D5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 42 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