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Q9Z6P6

- FUMC_CHLPN

UniProt

Q9Z6P6 - FUMC_CHLPN

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
Status
Reviewed - 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.
OMAiMESFNIH.
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 .
PIRi A72009.
B86617.
RefSeqi NP_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

ProteinModelPortali Q9Z6P6.
SMRi Q9Z6P6. Positions 1-456.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 115713.CPn1013.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD19150 ; AAD19150 ; CPn_1013 .
AAF38632 ; AAF38632 ; CP_0840 .
AAP98980 ; AAP98980 ; CpB1051 .
BAA99220 ; BAA99220 ; BAA99220 .
GeneIDi 1467730.
894645.
919783.
963045.
KEGGi cpa:CP0840.
cpj:CPj1013.
cpn:CPn1013.
cpt:CpB1051.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi MESFNIH.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci CPNE115711:GI7B-867-MONOMER.
CPNE115713:GHEY-1057-MONOMER.
CPNE138677:GH8N-1047-MONOMER.
CPNE182082:GH4N-1086-MONOMER.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00743. FumaraseC.
InterProi IPR005677. 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 ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00979. fumC_II. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 1, 2014
This is version 94 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