SubmitCancel

Skip Header

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

O84863

- FUMC_CHLTR

UniProt

O84863 - FUMC_CHLTR

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Fumarate hydratase class II
Gene
fumC, CT_855
Organism
Chlamydia trachomatis (strain D/UW-3/Cx)
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.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei185 – 1851Proton donor/acceptor By similarity
Active sitei315 – 3151 By similarity
Binding sitei316 – 3161Substrate By similarity
Sitei328 – 3281Important for catalytic activity By 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

UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class II (EC:4.2.1.2)
Short name:
Fumarase C
Gene namesi
Name:fumC
Ordered Locus Names:CT_855
OrganismiChlamydia trachomatis (strain D/UW-3/Cx)
Taxonomic identifieri272561 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000431: Chromosome

Subcellular locationi

Cytoplasm By similarity 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 – 463463Fumarate hydratase class IIUniRule annotation
PRO_0000161269Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi272561.CT855.

Structurei

3D structure databases

ProteinModelPortaliO84863.
SMRiO84863. Positions 1-456.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni95 – 973Substrate binding By similarity
Regioni126 – 1294B site By similarity
Regioni136 – 1383Substrate binding By similarity
Regioni184 – 1852Substrate binding By similarity
Regioni321 – 3233Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
KOiK01679.
OMAiIAFNDNC.
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.

O84863-1 [UniParc]FASTAAdd to Basket

« Hide

MRQENDSLGI VLVPEDKLFG AQTGRSQEFF SYGKESMPLE IIHALVKIKK    50
CAAKANGDLG CLDAKRRDMI VAATDEILSG EFDEHFPLKV WQTGSGTQSN 100
MNVNEVIANL AIQRHGGELG SKHPVHPNDH VNKSQSSNDV FPTAMHIAAV 150
QSIKGSLIPA LEHLKKVIDA KALEFARDIK IGRTHLMDAV PMTLGQEFSG 200
YSCQLHNCLE RIGFSLTHLY ELAIGGTAIG TGLNVPEGFV EKVIQYLRRE 250
TGEPFVPASN YFAALSNHDA LVQAHGSLTV LACALVKIAT DLSFLGSGPR 300
CGLGEIFFPE NEPGSSIMPG KINPTQSEAL QMVCSQVIGN NQSIIFSGTK 350
GNFELNVMKP VIIYDFLQSV NLLAGAMRSF ADYFVCGLKV NKGQLQQNVE 400
RSLMLVTALA PVLGYDKCSK IALKAFHENL SLKEACVSLG FLSEKEFDEH 450
VIPGLMVGNR GHE 463
Length:463
Mass (Da):50,339
Last modified:November 1, 1998 - v1
Checksum:i428E3DA10A839853
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE001273 Genomic DNA. Translation: AAC68452.1.
PIRiH71462.
RefSeqiNP_220377.1. NC_000117.1.

Genome annotation databases

EnsemblBacteriaiAAC68452; AAC68452; CT_855.
GeneIDi884656.
KEGGictr:CT_855.
PATRICi20381432. VBIChlTra43535_0944.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE001273 Genomic DNA. Translation: AAC68452.1 .
PIRi H71462.
RefSeqi NP_220377.1. NC_000117.1.

3D structure databases

ProteinModelPortali O84863.
SMRi O84863. Positions 1-456.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272561.CT855.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC68452 ; AAC68452 ; CT_855 .
GeneIDi 884656.
KEGGi ctr:CT_855.
PATRICi 20381432. VBIChlTra43535_0944.

Phylogenomic databases

eggNOGi COG0114.
KOi K01679.
OMAi IAFNDNC.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .

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. "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis."
    Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.
    Science 282:754-759(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: D/UW-3/Cx.

Entry informationi

Entry nameiFUMC_CHLTR
AccessioniPrimary (citable) accession number: O84863
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: November 1, 1998
Last modified: May 14, 2014
This is version 83 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.

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference 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