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O84863

- FUMC_CHLTR

UniProt

O84863 - FUMC_CHLTR

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Protein

Fumarate hydratase class II

Gene

fumC

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

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

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:CT_855
OrganismiChlamydia trachomatis (strain D/UW-3/Cx)
Taxonomic identifieri272561 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000431: 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 – 463463Fumarate hydratase class IIPRO_0000161269Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi272561.CT855.

Structurei

3D structure databases

ProteinModelPortaliO84863.
SMRiO84863. 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.
InParanoidiO84863.
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

        10         20         30         40         50
MRQENDSLGI VLVPEDKLFG AQTGRSQEFF SYGKESMPLE IIHALVKIKK
60 70 80 90 100
CAAKANGDLG CLDAKRRDMI VAATDEILSG EFDEHFPLKV WQTGSGTQSN
110 120 130 140 150
MNVNEVIANL AIQRHGGELG SKHPVHPNDH VNKSQSSNDV FPTAMHIAAV
160 170 180 190 200
QSIKGSLIPA LEHLKKVIDA KALEFARDIK IGRTHLMDAV PMTLGQEFSG
210 220 230 240 250
YSCQLHNCLE RIGFSLTHLY ELAIGGTAIG TGLNVPEGFV EKVIQYLRRE
260 270 280 290 300
TGEPFVPASN YFAALSNHDA LVQAHGSLTV LACALVKIAT DLSFLGSGPR
310 320 330 340 350
CGLGEIFFPE NEPGSSIMPG KINPTQSEAL QMVCSQVIGN NQSIIFSGTK
360 370 380 390 400
GNFELNVMKP VIIYDFLQSV NLLAGAMRSF ADYFVCGLKV NKGQLQQNVE
410 420 430 440 450
RSLMLVTALA PVLGYDKCSK IALKAFHENL SLKEACVSLG FLSEKEFDEH
460
VIPGLMVGNR GHE
Length:463
Mass (Da):50,339
Last modified:November 1, 1998 - v1
Checksum:i428E3DA10A839853
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi O84863.
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: October 29, 2014
This is version 85 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, 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