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Q9Z6P6 (FUMC_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:CPn_1013, CP_0840, CpB1051
OrganismChlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]
Taxonomic identifier83558 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length460 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. HAMAP-Rule MF_00743

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 termAllosteric enzyme
Complete 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 – 460460Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161268

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
Q9Z6P6 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: A59DA2D41F2100F1

FASTA46050,441
        10         20         30         40         50         60 
MRQEKDSLGI VEVPEDKLYG AQTMRSRNFF SWGPELMPYE VIRALVWIKK CAAQANQDLG 

        70         80         90        100        110        120 
FLDSKHCDMI VAAADEILEG GFEEHFPLKV WQTGSGTQSN MNVNEVIANL AIRHHGGVLG 

       130        140        150        160        170        180 
SKDPIHPNDH VNKSQSSNDV FPTAMHIAAV ISLKNKLIPA LDHMIRVLDA KVEEFRHDVK 

       190        200        210        220        230        240 
IGRTHLMDAV PMTLGQEFSG YSSQLRHCLE SIAFSLAHLY ELAIGATAVG TGLNVPEGFV 

       250        260        270        280        290        300 
EKIIHYLRKE TDEPFIPASN YFSALSCHDA LVDAHGSLAT LACALTKIAT DLSFLGSGPR 

       310        320        330        340        350        360 
CGLGELFFPE NEPGSSIMPG KVNPTQCEAL QMVCAQVLGN NQTVIIGGSR GNFELNVMKP 

       370        380        390        400        410        420 
VIIYNFLQSV DLLSEGMRAF SEFFVKGLKV NKARLQDNIN NSLMLVTALA PVLGYDKCSK 

       430        440        450        460 
AALKAFHESI SLKEACLALG YLSEKEFDRL VVPENMVGNH 

« Hide

References

[1]"Comparative genomes of Chlamydia pneumoniae and C. trachomatis."
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.
Nat. Genet. 21:385-389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CWL029.
[2]"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. expand/collapse author list , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AR39.
[3]"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J138.
[4]"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW-183.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001363 Genomic DNA. Translation: AAD19150.1.
AE002161 Genomic DNA. Translation: AAF38632.1.
BA000008 Genomic DNA. Translation: BAA99220.1.
AE009440 Genomic DNA. Translation: AAP98980.1.
PIRA72009.
B86617.
RefSeqNP_225207.1. NC_000922.1.
NP_301068.1. NC_002491.1.
NP_445379.1. NC_002179.2.
NP_877323.1. NC_005043.1.

3D structure databases

ProteinModelPortalQ9Z6P6.
SMRQ9Z6P6. Positions 1-456.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING115713.CPn1013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD19150; AAD19150; CPn_1013.
AAF38632; AAF38632; CP_0840.
AAP98980; AAP98980; CpB1051.
BAA99220; BAA99220; BAA99220.
GeneID1467730.
894645.
919783.
963045.
KEGGcpa:CP0840.
cpj:CPj1013.
cpn:CPn1013.
cpt:CpB1051.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMARIEKDTM.
OrthoDBEOG6V1M4M.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycCPNE115711:GI7B-867-MONOMER.
CPNE115713:GHEY-1057-MONOMER.
CPNE138677:GH8N-1047-MONOMER.
CPNE182082:GH4N-1086-MONOMER.
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...

Entry information

Entry nameFUMC_CHLPN
AccessionPrimary (citable) accession number: Q9Z6P6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: May 1, 1999
Last modified: March 19, 2014
This is version 92 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

PATHWAY comments

Index of metabolic and biosynthesis pathways