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Reviewed, UniProtKB/Swiss-Prot Q9PL64 (FUMC_CHLMU)

Last modified November 3, 2009. Version 49. 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: TC_0244
OrganismChlamydia muridarum [Complete proteome] [HAMAP]
Taxonomic identifier83560 [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_0000161267

Regions

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

Sites

Binding site971Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PL64-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7F3C5EA2F2991332

FASTA46350,428
        10         20         30         40         50         60 
MRQENDSLGI VMVPEDKLFG AQTGRSKNFF SYGKELMPIE VIQALVKIKK CAAKANGDLQ 

        70         80         90        100        110        120 
CLDAKRRDMI VAASDEILSG GLEEHFPLKV WQTGSGTQSN MNVNEVIANL AIKRHGGELG 

       130        140        150        160        170        180 
SKNPVHPNDH VNKSQSSNDV FPTAMHIAAV QSIKGSLIPA LEHLQKNLDA KALEFSRDIK 

       190        200        210        220        230        240 
IGRTHLMDAV PMTLGQEFSG YSHQLRSCLE RIGFSLTHLY ELAIGGTAVG TGLNVPEGFV 

       250        260        270        280        290        300 
DKVIYYLRQE TGEPFIPASN YFAALSNHDA LVQAHGSLAV LACSLIKIAT DLSFLGSGPR 

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

       370        380        390        400        410        420 
VIIYDFLQSV NLLSGAMRSF ADYFVSGLKV NRGQLQQNVE RSLMLVTALA PVLGYDKCSK 

       430        440        450        460 
IALKAFHENL SLKEACVSLG FLSEQEFDTH VVPGLMLGKR ERE 

« Hide

Cross-references

Sequence databases

AE002160 Genomic DNA. Translation: AAF39114.1.
PIRB81725.
RefSeqNP_296623.1.

3D structure databases

HSSPHSSP built from PDB template 1YFM based on UniProtKB P08417.
ModBaseSearch...

Genome annotation databases

GeneID1246413.
GenomeReviewsGene locus TC_0244 in contig AE002160_GR.
KEGGcmu:TC0244.
TIGRTC_0244.

Phylogenomic databases

HOGENOMQ9PL64.
OMAGSQGHFE.

Enzyme and pathway databases

BioCycCMUR243161:TC_0244-MON.
BRENDA4.2.1.2. 256349.

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_CHLMU
AccessionPrimary (citable) accession number: Q9PL64
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2000
Last modified: November 3, 2009
This is version 49 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