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Protein

C-1-tetrahydrofolate synthase, mitochondrial

Gene

MIS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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.

Pathway:itetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.
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 sitei226 – 2261NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi201 – 2033NADPBy similarity
Nucleotide bindingi408 – 4158ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • formate-tetrahydrofolate ligase activity Source: SGD
  • methenyltetrahydrofolate cyclohydrolase activity Source: SGD
  • methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: SGD

GO - Biological processi

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:YBR084W-MONOMER.
BRENDAi3.5.4.9. 984.
ReactomeiREACT_324954. Metabolism of folate and pterines.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
C-1-tetrahydrofolate synthase, mitochondrial
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:MIS1
Ordered Locus Names:YBR084W
ORF Names:YBR0751
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome II

Organism-specific databases

CYGDiYBR084w.
EuPathDBiFungiDB:YBR084W.
SGDiS000000288. MIS1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434Mitochondrion1 PublicationAdd
BLAST
Chaini35 – 975941C-1-tetrahydrofolate synthase, mitochondrialPRO_0000034052Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei346 – 3461PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP09440.
PaxDbiP09440.
PeptideAtlasiP09440.
PRIDEiP09440.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RPB5P204341EBI-3903,EBI-15781
SAT4P253331EBI-3903,EBI-16492
YHR080CP388001EBI-3903,EBI-24597

Protein-protein interaction databases

BioGridi32788. 96 interactions.
DIPiDIP-6724N.
IntActiP09440. 50 interactions.
MINTiMINT-660665.

Structurei

3D structure databases

ProteinModelPortaliP09440.
SMRiP09440. Positions 37-326, 344-975.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 343309Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseAdd
BLAST
Regioni83 – 875Substrate bindingBy similarity
Regioni130 – 1323Substrate bindingBy similarity
Regioni301 – 3055Substrate bindingBy similarity
Regioni344 – 975632Formyltetrahydrofolate 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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0190.
GeneTreeiENSGT00800000124409.
HOGENOMiHOG000040280.
InParanoidiP09440.
KOiK00288.
OMAiLPTHAGF.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09440-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRLSLLSN SRAFQQARWR IYRLKVSPTV HASQYHILSG RKLAQSIREK
60 70 80 90 100
ANDEIQAIKL KHPNFKPTLK IIQVGARPDS STYVRMKLKA SKDSNVDCII
110 120 130 140 150
EKLPAEITEV ELLKKISDIN DDDSIHGLLI QLPLPRHLDE TTITNAVDFK
160 170 180 190 200
KDVDGFHRYN AGELAKKGGK PYFIPCTPYG CMKLLEEAHV KLDGKNAVVL
210 220 230 240 250
GRSSIVGNPI ASLLKNANAT VTVCHSHTRN IAEVVSQADI VIAACGIPQY
260 270 280 290 300
VKSDWIKEGA VVIDVGINYV PDISKKSGQK LVGDVDFDSV KEKTSYITPV
310 320 330 340 350
PGGVGPMTVA MLVSNVLLAA KRQFVESEKL PVIKPLPLHL ESPVPSDIDI
360 370 380 390 400
SRAQSPKHIK QVAEELGIHS HELELYGHYK AKISPNIFKR LESRENGKYV
410 420 430 440 450
LVAGITPTPL GEGKSTTTMG LVQALSAHLG KPSIANVRQP SLGPTLGVKG
460 470 480 490 500
GAAGGGYAQV IPMDEFNLHL TGDIHAISAA NNLLAAAIDT RMFHEATQKN
510 520 530 540 550
DSTFYKRLVP RKKGIRKFTP SMQRRLKRLD IEKEDPDALT PEEVKRFARL
560 570 580 590 600
NINPDTITIR RVVDINDRML RQITIGEAAT EKGFTRTTGF DITVASELMA
610 620 630 640 650
ILALSKSLHE MKERIGRMVI GADYDNKPVT VEDIGCTGAL TALLRDAIKP
660 670 680 690 700
NLMQTLEGTP VMVHAGPFAN ISIGASSVIA DLMALKLVGS EKNPLNDKNI
710 720 730 740 750
HEPGYVVTEA GFDFAMGGER FFDIKCRSSG LVPDAVVLVA TVRALKSHGG
760 770 780 790 800
APNVKPGQSL PKEYTEENID FVAKGVSNLV KQIENIKTFG IPVVVAINRF
810 820 830 840 850
ETDSQAEIEV IKKAALNAGA SHAVTSNHWM EGGKGAVELA HAVVDATKEP
860 870 880 890 900
KNFNFLYDVN SSIEDKLTSI VQKMYGGAKI EVSPEAQKKI DTYKKQGFGN
910 920 930 940 950
LPICIAKTQY SLSHDPSLKG VPRGFTFPIR DVRASIGAGY LYALAAEIQT
960 970
IPGLSTYAGY MAVEVDDDGE IEGLF
Length:975
Mass (Da):106,217
Last modified:July 1, 1989 - v1
Checksum:iB9421D4F8981531F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35953 Genomic DNA. Translation: CAA85029.1.
J03724 Genomic DNA. Translation: AAA34781.1.
BK006936 Genomic DNA. Translation: DAA07203.1.
PIRiA28174.
RefSeqiNP_009640.1. NM_001178432.1.

Genome annotation databases

EnsemblFungiiYBR084W; YBR084W; YBR084W.
GeneIDi852378.
KEGGisce:YBR084W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35953 Genomic DNA. Translation: CAA85029.1.
J03724 Genomic DNA. Translation: AAA34781.1.
BK006936 Genomic DNA. Translation: DAA07203.1.
PIRiA28174.
RefSeqiNP_009640.1. NM_001178432.1.

3D structure databases

ProteinModelPortaliP09440.
SMRiP09440. Positions 37-326, 344-975.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32788. 96 interactions.
DIPiDIP-6724N.
IntActiP09440. 50 interactions.
MINTiMINT-660665.

Proteomic databases

MaxQBiP09440.
PaxDbiP09440.
PeptideAtlasiP09440.
PRIDEiP09440.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR084W; YBR084W; YBR084W.
GeneIDi852378.
KEGGisce:YBR084W.

Organism-specific databases

CYGDiYBR084w.
EuPathDBiFungiDB:YBR084W.
SGDiS000000288. MIS1.

Phylogenomic databases

eggNOGiCOG0190.
GeneTreeiENSGT00800000124409.
HOGENOMiHOG000040280.
InParanoidiP09440.
KOiK00288.
OMAiLPTHAGF.
OrthoDBiEOG7K0ZMJ.

Enzyme and pathway databases

UniPathwayiUPA00193.
BioCyciYEAST:YBR084W-MONOMER.
BRENDAi3.5.4.9. 984.
ReactomeiREACT_324954. Metabolism of folate and pterines.

Miscellaneous databases

NextBioi971174.
PROiP09440.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the Saccharomyces cerevisiae MIS1 gene encoding mitochondrial C1-tetrahydrofolate synthase."
    Shannon K.W., Rabinowitz J.C.
    J. Biol. Chem. 263:7717-7725(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Purification and characterization of a mitochondrial isozyme of C1-tetrahydrofolate synthase from Saccharomyces cerevisiae."
    Shannon K.W., Rabinowitz J.C.
    J. Biol. Chem. 261:12266-12271(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 35-74, CHARACTERIZATION, SUBCELLULAR LOCATION, SUBUNIT.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.

Entry informationi

Entry nameiC1TM_YEAST
AccessioniPrimary (citable) accession number: P09440
Secondary accession number(s): D6VQ83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 22, 2015
This is version 150 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 11400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

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 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.