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Protein

Bifunctional protein FolD

Gene

folD

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.UniRule annotation

Catalytic activityi

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH.UniRule annotation
5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.UniRule annotation

Pathwayi: tetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei182 – 1821NADPUniRule annotation1 Publication
Binding sitei223 – 2231NADP; via amide nitrogenUniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi157 – 1593NADPUniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis, Methionine biosynthesis, One-carbon metabolism, Purine biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.5.1.5. 6324.
3.5.4.9. 6324.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein FolDUniRule annotation
Including the following 2 domains:
Methylenetetrahydrofolate dehydrogenaseUniRule annotation (EC:1.5.1.5UniRule annotation)
Methenyltetrahydrofolate cyclohydrolaseUniRule annotation (EC:3.5.4.9UniRule annotation)
Gene namesi
Name:folDUniRule annotation
Ordered Locus Names:Ta0898
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
Proteomesi
  • UP000001024 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 276276Bifunctional protein FolDPRO_0000199318Add
BLAST

Proteomic databases

PRIDEiQ05213.

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi273075.Ta0898.

Structurei

Secondary structure

1
276
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2317Combined sources
Beta strandi29 – 368Combined sources
Helixi39 – 5517Combined sources
Beta strandi58 – 669Combined sources
Helixi69 – 8113Combined sources
Beta strandi87 – 904Combined sources
Helixi100 – 1045Combined sources
Helixi109 – 1113Combined sources
Helixi118 – 1258Combined sources
Helixi134 – 14613Combined sources
Beta strandi152 – 1565Combined sources
Turni160 – 1623Combined sources
Helixi163 – 17210Combined sources
Beta strandi176 – 1805Combined sources
Helixi187 – 1937Combined sources
Beta strandi194 – 1996Combined sources
Helixi209 – 2113Combined sources
Beta strandi217 – 2204Combined sources
Beta strandi224 – 2263Combined sources
Beta strandi229 – 2313Combined sources
Helixi236 – 2405Combined sources
Beta strandi243 – 2464Combined sources
Turni249 – 2513Combined sources
Helixi254 – 2563Combined sources
Helixi257 – 27519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NGLX-ray2.40A/C1-276[»]
3NGXX-ray2.30A/B1-276[»]
ProteinModelPortaliQ05213.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05213.

Family & Domainsi

Sequence similaritiesi

Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04538. Archaea.
COG0190. LUCA.
HOGENOMiHOG000218242.
KOiK01491.
OMAiLMFNTIK.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01576. THF_DHG_CYH.
InterProiIPR016040. NAD(P)-bd_dom.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamiPF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05213-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKILRGEEIA EKKAENLHGI IERSGLEPSL KLIQIGDNEA ASIYARAKIR
60 70 80 90 100
RGKKIGIAVD LEKYDDISMK DLLKRIDDLA KDPQINGIMI ENPLPKGFDY
110 120 130 140 150
YEIVRNIPYY KDVDALSPYN QGLIALNREF LVPATPRAVI DIMDYYGYHE
160 170 180 190 200
NTVTIVNRSP VVGRPLSMML LNRNYTVSVC HSKTKDIGSM TRSSKIVVVA
210 220 230 240 250
VGRPGFLNRE MVTPGSVVID VGINYVNDKV VGDANFEDLS EYVEAITPVP
260 270
GGVGPITATN ILENVVKAAE FQKNNL
Length:276
Mass (Da):30,622
Last modified:December 1, 2000 - v2
Checksum:i55DFA04ADBCBF907
GO

Sequence cautioni

The sequence CAA42451.1 differs from that shown. Reason: Frameshift at position 58. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445065 Genomic DNA. Translation: CAC12027.1.
X59788 Genomic DNA. Translation: CAA42451.1. Frameshift.
PIRiS29789.
RefSeqiWP_010901308.1. NC_002578.1.

Genome annotation databases

EnsemblBacteriaiCAC12027; CAC12027; CAC12027.
GeneIDi1456434.
KEGGitac:Ta0898.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445065 Genomic DNA. Translation: CAC12027.1.
X59788 Genomic DNA. Translation: CAA42451.1. Frameshift.
PIRiS29789.
RefSeqiWP_010901308.1. NC_002578.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NGLX-ray2.40A/C1-276[»]
3NGXX-ray2.30A/B1-276[»]
ProteinModelPortaliQ05213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273075.Ta0898.

Proteomic databases

PRIDEiQ05213.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC12027; CAC12027; CAC12027.
GeneIDi1456434.
KEGGitac:Ta0898.

Phylogenomic databases

eggNOGiarCOG04538. Archaea.
COG0190. LUCA.
HOGENOMiHOG000218242.
KOiK01491.
OMAiLMFNTIK.

Enzyme and pathway databases

UniPathwayiUPA00193.
BRENDAi1.5.1.5. 6324.
3.5.4.9. 6324.

Miscellaneous databases

EvolutionaryTraceiQ05213.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01576. THF_DHG_CYH.
InterProiIPR016040. NAD(P)-bd_dom.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamiPF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
    Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
    Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  2. "Cloning, sequencing and expression of the gene encoding glucose dehydrogenase from the thermophilic archaeon Thermoplasma acidophilum."
    Bright J.R., Byrom D., Danson M.J., Hough D.W., Towner P.
    Eur. J. Biochem. 211:549-554(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  3. "Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum."
    Lee W.H., Sung M.W., Kim J.H., Kim Y.K., Han A., Hwang K.Y.
    Biochem. Biophys. Res. Commun. 406:459-463(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.

Entry informationi

Entry nameiFOLD_THEAC
AccessioniPrimary (citable) accession number: Q05213
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 1, 2000
Last modified: March 16, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.