Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fumarate hydratase class II

Gene

fumC

Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reversible addition of water to fumarate to give L-malate.By similarity

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei185 – 1851Proton donor/acceptorBy similarity
Active sitei315 – 3151By similarity
Binding sitei316 – 3161SubstrateUniRule annotation
Sitei328 – 3281Important for catalytic activityBy similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fumarate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciCPNE115711:GI7B-867-MONOMER.
CPNE115713:GHEY-1057-MONOMER.
CPNE138677:GH8N-1047-MONOMER.
CPNE182082:GH4N-1086-MONOMER.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class IIUniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase CUniRule annotation
Gene namesi
Name:fumCUniRule annotation
Ordered Locus Names:CPn_1013, CP_0840, CpB1051
OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)
Taxonomic identifieri83558 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000424: Chromosome, UP000000583: Chromosome, UP000000801: Chromosome, UP000000802: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 460460Fumarate hydratase class IIPRO_0000161268Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi115713.CPn1013.

Structurei

3D structure databases

ProteinModelPortaliQ9Z6P6.
SMRiQ9Z6P6. Positions 1-456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni95 – 973Substrate bindingUniRule annotation
Regioni126 – 1294B siteUniRule annotation
Regioni136 – 1383Substrate bindingUniRule annotation
Regioni184 – 1852Substrate bindingUniRule annotation
Regioni321 – 3233Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiNTPKGYD.
OrthoDBiEOG6V1M4M.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. 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]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z6P6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRQEKDSLGI VEVPEDKLYG AQTMRSRNFF SWGPELMPYE VIRALVWIKK
60 70 80 90 100
CAAQANQDLG FLDSKHCDMI VAAADEILEG GFEEHFPLKV WQTGSGTQSN
110 120 130 140 150
MNVNEVIANL AIRHHGGVLG SKDPIHPNDH VNKSQSSNDV FPTAMHIAAV
160 170 180 190 200
ISLKNKLIPA LDHMIRVLDA KVEEFRHDVK IGRTHLMDAV PMTLGQEFSG
210 220 230 240 250
YSSQLRHCLE SIAFSLAHLY ELAIGATAVG TGLNVPEGFV EKIIHYLRKE
260 270 280 290 300
TDEPFIPASN YFSALSCHDA LVDAHGSLAT LACALTKIAT DLSFLGSGPR
310 320 330 340 350
CGLGELFFPE NEPGSSIMPG KVNPTQCEAL QMVCAQVLGN NQTVIIGGSR
360 370 380 390 400
GNFELNVMKP VIIYNFLQSV DLLSEGMRAF SEFFVKGLKV NKARLQDNIN
410 420 430 440 450
NSLMLVTALA PVLGYDKCSK AALKAFHESI SLKEACLALG YLSEKEFDRL
460
VVPENMVGNH
Length:460
Mass (Da):50,441
Last modified:May 1, 1999 - v1
Checksum:iA59DA2D41F2100F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001363 Genomic DNA. Translation: AAD19150.1.
AE002161 Genomic DNA. Translation: AAF38632.1.
BA000008 Genomic DNA. Translation: BAA99220.1.
AE009440 Genomic DNA. Translation: AAP98980.1.
PIRiA72009.
B86617.
RefSeqiNP_225207.1. NC_000922.1.
NP_301068.1. NC_002491.1.
NP_445379.1. NC_002179.2.
NP_877323.1. NC_005043.1.

Genome annotation databases

EnsemblBacteriaiAAD19150; AAD19150; CPn_1013.
AAF38632; AAF38632; CP_0840.
AAP98980; AAP98980; CpB1051.
BAA99220; BAA99220; BAA99220.
GeneIDi1467730.
894645.
919783.
963045.
KEGGicpa:CP0840.
cpj:CPj1013.
cpn:CPn1013.
cpt:CpB1051.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001363 Genomic DNA. Translation: AAD19150.1.
AE002161 Genomic DNA. Translation: AAF38632.1.
BA000008 Genomic DNA. Translation: BAA99220.1.
AE009440 Genomic DNA. Translation: AAP98980.1.
PIRiA72009.
B86617.
RefSeqiNP_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

ProteinModelPortaliQ9Z6P6.
SMRiQ9Z6P6. Positions 1-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi115713.CPn1013.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD19150; AAD19150; CPn_1013.
AAF38632; AAF38632; CP_0840.
AAP98980; AAP98980; CpB1051.
BAA99220; BAA99220; BAA99220.
GeneIDi1467730.
894645.
919783.
963045.
KEGGicpa:CP0840.
cpj:CPj1013.
cpn:CPn1013.
cpt:CpB1051.

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiNTPKGYD.
OrthoDBiEOG6V1M4M.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciCPNE115711:GI7B-867-MONOMER.
CPNE115713:GHEY-1057-MONOMER.
CPNE138677:GH8N-1047-MONOMER.
CPNE182082:GH4N-1086-MONOMER.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. 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]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CWL029.
  2. 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.

Entry informationi

Entry nameiFUMC_CHLPN
AccessioniPrimary (citable) accession number: Q9Z6P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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).By similarity

Keywords - Technical termi

Allosteric enzyme, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.