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O66271

- FUMC_THET2

UniProt

O66271 - FUMC_THET2

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
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 sitei188 – 1881Proton donor/acceptorBy similarity
Active sitei318 – 3181By similarity
Binding sitei319 – 3191SubstrateUniRule annotation
Sitei331 – 3311Important 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

BioCyciTTHE262724:GCAT-194-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:TT_C0190
OrganismiThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Taxonomic identifieri262724 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000592: 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 – 466466Fumarate hydratase class IIPRO_0000161327Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi262724.TTC0190.

Structurei

3D structure databases

ProteinModelPortaliO66271.
SMRiO66271. Positions 4-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1013Substrate bindingUniRule annotation
Regioni129 – 1324B siteUniRule annotation
Regioni139 – 1413Substrate bindingUniRule annotation
Regioni187 – 1882Substrate bindingUniRule annotation
Regioni324 – 3263Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
KOiK01679.
OMAiGYLEAKI.
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.

O66271-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEYRIERDTM GEVRVPADKY WGAQTQRSLE NFRIGTDRFR MPLEIIRAYG
60 70 80 90 100
MLKKAAARAN LELGELPEEI AKAIIQAAEE VVQGKWDDHF PLVVFQTGSG
110 120 130 140 150
TQTNMNVNEV IANRASEILG KPLGSKYVHP NDHVNRGQSS NDTFPTAMYV
160 170 180 190 200
AVALALHQRL YPAVEGLIRT FTAKAQAFDQ IVKVGRTHLM DAVPITLGQE
210 220 230 240 250
IGSWAAQLKT TLAAVKEMEK GLYNLAIGGT AVGTGLNAHP RFGELVAKYL
260 270 280 290 300
AEETGLPFRV AENRFAALAA HDELVNVMGA IRTLAGALMK IGNDVRWLAS
310 320 330 340 350
GPYAGIGEIT IPANEPGSSI MPGKVNPTQV EALTMVVVRV YGNDHTVAFA
360 370 380 390 400
GSQGNFQLNV YKPVMAYSTL ESINLLADAV ASFDAHLAQG IEPNLERIEE
410 420 430 440 450
HLQKNPMLAT ALNKAIGYDK AAEIVKKALK EKKTLKQAAL ELGYLTEEEF
460
DRIVVPMRLA KPHEGA
Length:466
Mass (Da):50,882
Last modified:May 24, 2004 - v2
Checksum:iC0ED1307333A65A8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341I → F in BAA25700. 1 PublicationCurated
Sequence conflicti238 – 2381A → G in BAA25700. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010884 Genomic DNA. Translation: BAA25700.1.
AE017221 Genomic DNA. Translation: AAS80538.1.
PIRiT43727.
RefSeqiYP_004165.1. NC_005835.1.

Genome annotation databases

EnsemblBacteriaiAAS80538; AAS80538; TT_C0190.
GeneIDi2774678.
KEGGitth:TTC0190.
PATRICi23950773. VBITheThe54392_0191.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010884 Genomic DNA. Translation: BAA25700.1 .
AE017221 Genomic DNA. Translation: AAS80538.1 .
PIRi T43727.
RefSeqi YP_004165.1. NC_005835.1.

3D structure databases

ProteinModelPortali O66271.
SMRi O66271. Positions 4-463.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 262724.TTC0190.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAS80538 ; AAS80538 ; TT_C0190 .
GeneIDi 2774678.
KEGGi tth:TTC0190.
PATRICi 23950773. VBITheThe54392_0191.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci TTHE262724:GCAT-194-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

« Hide 'large scale' publications
  1. "Molecular cloning and sequence analysis of the fumC and sodA genes from an extremely thermophilic eubacterium Thermus thermophilus."
    Kosuge T., Umehara K., Matsuura S., Hoshino T.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB27 / ATCC BAA-163 / DSM 7039.

Entry informationi

Entry nameiFUMC_THET2
AccessioniPrimary (citable) accession number: O66271
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: May 24, 2004
Last modified: November 26, 2014
This is version 91 of the entry and version 2 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