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P07245

- C1TC_YEAST

UniProt

P07245 - C1TC_YEAST

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Protein

C-1-tetrahydrofolate synthase, cytoplasmic

Gene

ADE3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH.
5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei194 – 1941NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi169 – 1713NADPBy similarity
Nucleotide bindingi384 – 3918ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. formate-tetrahydrofolate ligase activity Source: SGD
  3. methenyltetrahydrofolate cyclohydrolase activity Source: SGD
  4. methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: SGD

GO - Biological processi

  1. folic acid-containing compound biosynthetic process Source: InterPro
  2. folic acid-containing compound metabolic process Source: SGD
  3. histidine biosynthetic process Source: UniProtKB-KW
  4. methionine biosynthetic process Source: UniProtKB-KW
  5. purine nucleobase biosynthetic process Source: SGD
  6. purine nucleotide biosynthetic process Source: UniProtKB-KW
  7. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YGR204W-MONOMER.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
C-1-tetrahydrofolate synthase, cytoplasmic
Short name:
C1-THF synthase
Including the following 3 domains:
Methylenetetrahydrofolate dehydrogenase (EC:1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase (EC:3.5.4.9)
Formyltetrahydrofolate synthetase (EC:6.3.4.3)
Gene namesi
Name:ADE3
Ordered Locus Names:YGR204W
ORF Names:G7733
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR204w.
SGDiS000003436. ADE3.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111C → S: Almost no effect on activity. 1 Publication
Mutagenesisi144 – 1441C → S: Cyclohydrolase activity is reduced 20-fold. Dehydrogenase Km is increased 7-fold. 1 Publication
Mutagenesisi257 – 2571C → S: Cyclohydrolase activity is increased 2-fold. Dehydrogenase Km is increased 2-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 946946C-1-tetrahydrofolate synthase, cytoplasmicPRO_0000199326Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei176 – 1761Phosphoserine2 Publications
Modified residuei318 – 3181Phosphothreonine1 Publication
Modified residuei322 – 3221Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP07245.
PaxDbiP07245.
PeptideAtlasiP07245.

Expressioni

Gene expression databases

GenevestigatoriP07245.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi33457. 36 interactions.
DIPiDIP-3867N.
IntActiP07245. 11 interactions.
MINTiMINT-574376.
STRINGi4932.YGR204W.

Structurei

3D structure databases

ProteinModelPortaliP07245.
SMRiP07245. Positions 2-297, 320-946.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 319319Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseAdd
BLAST
Regioni51 – 555Substrate bindingBy similarity
Regioni98 – 1003Substrate bindingBy similarity
Regioni277 – 2815Substrate bindingBy similarity
Regioni320 – 946627Formyltetrahydrofolate synthetaseAdd
BLAST

Domaini

This trifunctional enzyme consists of two major domains: an N-terminal part containing the methylene-THF dehydrogenase and cyclohydrolase activities and a larger C-terminal part containing formyl-THF synthetase activity.

Sequence similaritiesi

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.Curated
In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.Curated

Phylogenomic databases

eggNOGiCOG0190.
GeneTreeiENSGT00750000117401.
HOGENOMiHOG000040280.
InParanoidiP07245.
KOiK00288.
OMAiHEYLDEN.
OrthoDBiEOG7K0ZMJ.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPiMF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProiIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamiPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07245-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGQVLDGKA CAQQFRSNIA NEIKSIQGHV PGFAPNLAII QVGNRPDSAT
60 70 80 90 100
YVRMKRKAAE EAGIVANFIH LDESATEFEV LRYVDQLNED PHTHGIIVQL
110 120 130 140 150
PLPAHLDEDR ITSRVLAEKD VDGFGPTNIG ELNKKNGHPF FLPCTPKGII
160 170 180 190 200
ELLHKANVTI EGSRSVVIGR SDIVGSPVAE LLKSLNSTVT ITHSKTRDIA
210 220 230 240 250
SYLHDADIVV VAIGQPEFVK GEWFKPRDGT SSDKKTVVID VGTNYVADPS
260 270 280 290 300
KKSGFKCVGD VEFNEAIKYV HLITPVPGGV GPMTVAMLMQ NTLIAAKRQM
310 320 330 340 350
EESSKPLQIP PLPLKLLTPV PSDIDISRAQ QPKLINQLAQ ELGIYSHELE
360 370 380 390 400
LYGHYKAKIS PKVIERLQTR QNGKYILVSG ITPTPLGEGK STTTMGLVQA
410 420 430 440 450
LTAHLGKPAI ANVRQPSLGP TLGVKGGAAG GGYSQVIPMD EFNLHLTGDI
460 470 480 490 500
HAIGAANNLL AAAIDTRMFH ETTQKNDATF YNRLVPRKNG KRKFTPSMQR
510 520 530 540 550
RLNRLGIQKT NPDDLTPEEI NKFARLNIDP DTITIKRVVD INDRMLRQIT
560 570 580 590 600
IGQAPTEKNH TRVTGFDITV ASELMAILAL SKDLRDMKER IGRVVVAADV
610 620 630 640 650
NRSPVTVEDV GCTGALTALL RDAIKPNLMQ TLEGTPVLVH AGPFANISIG
660 670 680 690 700
ASSVIADRVA LKLVGTEPEA KTEAGYVVTE AGFDFTMGGE RFFNIKCRSS
710 720 730 740 750
GLTPNAVVLV ATVRALKSHG GAPDVKPGQP LPSAYTEENI EFVEKGAANM
760 770 780 790 800
CKQIANIKQF GVPVVVAINK FETDTEGEIA AIRKAALEAG AFEAVTSNHW
810 820 830 840 850
AEGGKGAIDL AKAVIEASNQ PVDFHFLYDV NSSVEDKLTT IVQKMYGGAA
860 870 880 890 900
IDILPEAQRK IDMYKEQGFG NLPICIAKTQ YSLSHDATLK GVPTGFTFPI
910 920 930 940
RDVRLSNGAG YLYALAAEIQ TIPGLATYAG YMAVEVDDDG EIDGLF
Length:946
Mass (Da):102,205
Last modified:April 1, 1988 - v1
Checksum:iBC2897EC380CBA6F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12878 Genomic DNA. Translation: AAA66316.1.
Z49133 Genomic DNA. Translation: CAA88997.1.
Z72989 Genomic DNA. Translation: CAA97231.1.
AY692966 Genomic DNA. Translation: AAT92985.1.
BK006941 Genomic DNA. Translation: DAA08297.1.
PIRiA29550.
RefSeqiNP_011720.3. NM_001181333.3.

Genome annotation databases

EnsemblFungiiYGR204W; YGR204W; YGR204W.
GeneIDi853118.
KEGGisce:YGR204W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12878 Genomic DNA. Translation: AAA66316.1 .
Z49133 Genomic DNA. Translation: CAA88997.1 .
Z72989 Genomic DNA. Translation: CAA97231.1 .
AY692966 Genomic DNA. Translation: AAT92985.1 .
BK006941 Genomic DNA. Translation: DAA08297.1 .
PIRi A29550.
RefSeqi NP_011720.3. NM_001181333.3.

3D structure databases

ProteinModelPortali P07245.
SMRi P07245. Positions 2-297, 320-946.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33457. 36 interactions.
DIPi DIP-3867N.
IntActi P07245. 11 interactions.
MINTi MINT-574376.
STRINGi 4932.YGR204W.

Proteomic databases

MaxQBi P07245.
PaxDbi P07245.
PeptideAtlasi P07245.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR204W ; YGR204W ; YGR204W .
GeneIDi 853118.
KEGGi sce:YGR204W.

Organism-specific databases

CYGDi YGR204w.
SGDi S000003436. ADE3.

Phylogenomic databases

eggNOGi COG0190.
GeneTreei ENSGT00750000117401.
HOGENOMi HOG000040280.
InParanoidi P07245.
KOi K00288.
OMAi HEYLDEN.
OrthoDBi EOG7K0ZMJ.

Enzyme and pathway databases

UniPathwayi UPA00193 .
BioCyci YEAST:YGR204W-MONOMER.

Miscellaneous databases

NextBioi 973148.

Gene expression databases

Genevestigatori P07245.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPi MF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProi IPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view ]
Pfami PF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view ]
PRINTSi PR00085. THFDHDRGNASE.
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the Saccharomyces cerevisiae ADE3 gene encoding C1-tetrahydrofolate synthase."
    Staben C., Rabinowitz J.C.
    J. Biol. Chem. 261:4629-4637(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the yeast PMT and EF1G genes, of the human and bacterial electron-transferring flavoproteins (beta-chain) and of the Escherichia coli phosphoserine phosphohydrolase, and five new ORFs."
    Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A., Rodrigues-Pousada C.
    Yeast 12:273-280(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Site-directed mutagenesis of yeast C1-tetrahydrofolate synthase: analysis of an overlapping active site in a multifunctional enzyme."
    Barlowe C.K., Williams M.E., Rabinowitz J.C., Appling D.R.
    Biochemistry 28:2099-2106(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; THR-318 AND SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiC1TC_YEAST
AccessioniPrimary (citable) accession number: P07245
Secondary accession number(s): D6VUY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: October 29, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 35600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3