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O66271

- FUMC_THET2

UniProt

O66271 - FUMC_THET2

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Protein
Fumarate hydratase class II
Gene
fumC, TT_C0190
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.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei188 – 1881Proton donor/acceptor By similarity
Active sitei318 – 3181 By similarity
Binding sitei319 – 3191Substrate By similarity
Sitei331 – 3311Important 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

BioCyciTTHE262724:GCAT-194-MONOMER.
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:TT_C0190
OrganismiThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Taxonomic identifieri262724 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000592: 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 – 466466Fumarate hydratase class IIUniRule annotation
PRO_0000161327Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi262724.TTC0190.

Structurei

3D structure databases

ProteinModelPortaliO66271.
SMRiO66271. Positions 4-463.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1013Substrate binding By similarity
Regioni129 – 1324B site By similarity
Regioni139 – 1413Substrate binding By similarity
Regioni187 – 1882Substrate binding By similarity
Regioni324 – 3263Substrate binding By similarity

Sequence similaritiesi

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

MEYRIERDTM GEVRVPADKY WGAQTQRSLE NFRIGTDRFR MPLEIIRAYG    50
MLKKAAARAN LELGELPEEI AKAIIQAAEE VVQGKWDDHF PLVVFQTGSG 100
TQTNMNVNEV IANRASEILG KPLGSKYVHP NDHVNRGQSS NDTFPTAMYV 150
AVALALHQRL YPAVEGLIRT FTAKAQAFDQ IVKVGRTHLM DAVPITLGQE 200
IGSWAAQLKT TLAAVKEMEK GLYNLAIGGT AVGTGLNAHP RFGELVAKYL 250
AEETGLPFRV AENRFAALAA HDELVNVMGA IRTLAGALMK IGNDVRWLAS 300
GPYAGIGEIT IPANEPGSSI MPGKVNPTQV EALTMVVVRV YGNDHTVAFA 350
GSQGNFQLNV YKPVMAYSTL ESINLLADAV ASFDAHLAQG IEPNLERIEE 400
HLQKNPMLAT ALNKAIGYDK AAEIVKKALK EKKTLKQAAL ELGYLTEEEF 450
DRIVVPMRLA KPHEGA 466
Length:466
Mass (Da):50,882
Last modified:May 24, 2004 - v2
Checksum:iC0ED1307333A65A8
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB010884 Genomic DNA. Translation: BAA25700.1.
AE017221 Genomic DNA. Translation: AAS80538.1.
PIRiT43727.
RefSeqiWP_011172644.1. NC_005835.1.
YP_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:
EMBL
GenBank
DDBJ
Links Updated
AB010884 Genomic DNA. Translation: BAA25700.1 .
AE017221 Genomic DNA. Translation: AAS80538.1 .
PIRi T43727.
RefSeqi WP_011172644.1. NC_005835.1.
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: September 3, 2014
This is version 89 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.

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

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