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P09440 (C1TM_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-1-tetrahydrofolate synthase, mitochondrial

Short name=C1-THF synthase

Including the following 3 domains:

  1. Methylenetetrahydrofolate dehydrogenase
    EC=1.5.1.5
  2. Methenyltetrahydrofolate cyclohydrolase
    EC=3.5.4.9
  3. Formyltetrahydrofolate synthetase
    EC=6.3.4.3
Gene names
Name:MIS1
Ordered Locus Names:YBR084W
ORF Names:YBR0751
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length975 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH. HAMAP-Rule MF_01543

5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. HAMAP-Rule MF_01543

ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate. HAMAP-Rule MF_01543

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_01543

Subunit structure

Homodimer. Ref.4

Subcellular location

Mitochondrion Ref.4 Ref.5 Ref.7.

Domain

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. HAMAP-Rule MF_01543

Miscellaneous

Present with 11400 molecules/cell in log phase SD medium.

Sequence similarities

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion Ref.4
Chain35 – 975941C-1-tetrahydrofolate synthase, mitochondrial HAMAP-Rule MF_01543
PRO_0000034052

Regions

Nucleotide binding201 – 2033NADP By similarity
Nucleotide binding408 – 4158ATP By similarity
Region35 – 343309Methylenetetrahydrofolate dehydrogenase and cyclohydrolase HAMAP-Rule MF_01543
Region83 – 875Substrate binding By similarity
Region130 – 1323Substrate binding By similarity
Region301 – 3055Substrate binding By similarity
Region344 – 975632Formyltetrahydrofolate synthetase HAMAP-Rule MF_01543

Sites

Binding site2261NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
P09440 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: B9421D4F8981531F

FASTA975106,217
        10         20         30         40         50         60 
MLSRLSLLSN SRAFQQARWR IYRLKVSPTV HASQYHILSG RKLAQSIREK ANDEIQAIKL 

        70         80         90        100        110        120 
KHPNFKPTLK IIQVGARPDS STYVRMKLKA SKDSNVDCII EKLPAEITEV ELLKKISDIN 

       130        140        150        160        170        180 
DDDSIHGLLI QLPLPRHLDE TTITNAVDFK KDVDGFHRYN AGELAKKGGK PYFIPCTPYG 

       190        200        210        220        230        240 
CMKLLEEAHV KLDGKNAVVL GRSSIVGNPI ASLLKNANAT VTVCHSHTRN IAEVVSQADI 

       250        260        270        280        290        300 
VIAACGIPQY VKSDWIKEGA VVIDVGINYV PDISKKSGQK LVGDVDFDSV KEKTSYITPV 

       310        320        330        340        350        360 
PGGVGPMTVA MLVSNVLLAA KRQFVESEKL PVIKPLPLHL ESPVPSDIDI SRAQSPKHIK 

       370        380        390        400        410        420 
QVAEELGIHS HELELYGHYK AKISPNIFKR LESRENGKYV LVAGITPTPL GEGKSTTTMG 

       430        440        450        460        470        480 
LVQALSAHLG KPSIANVRQP SLGPTLGVKG GAAGGGYAQV IPMDEFNLHL TGDIHAISAA 

       490        500        510        520        530        540 
NNLLAAAIDT RMFHEATQKN DSTFYKRLVP RKKGIRKFTP SMQRRLKRLD IEKEDPDALT 

       550        560        570        580        590        600 
PEEVKRFARL NINPDTITIR RVVDINDRML RQITIGEAAT EKGFTRTTGF DITVASELMA 

       610        620        630        640        650        660 
ILALSKSLHE MKERIGRMVI GADYDNKPVT VEDIGCTGAL TALLRDAIKP NLMQTLEGTP 

       670        680        690        700        710        720 
VMVHAGPFAN ISIGASSVIA DLMALKLVGS EKNPLNDKNI HEPGYVVTEA GFDFAMGGER 

       730        740        750        760        770        780 
FFDIKCRSSG LVPDAVVLVA TVRALKSHGG APNVKPGQSL PKEYTEENID FVAKGVSNLV 

       790        800        810        820        830        840 
KQIENIKTFG IPVVVAINRF ETDSQAEIEV IKKAALNAGA SHAVTSNHWM EGGKGAVELA 

       850        860        870        880        890        900 
HAVVDATKEP KNFNFLYDVN SSIEDKLTSI VQKMYGGAKI EVSPEAQKKI DTYKKQGFGN 

       910        920        930        940        950        960 
LPICIAKTQY SLSHDPSLKG VPRGFTFPIR DVRASIGAGY LYALAAEIQT IPGLSTYAGY 

       970 
MAVEVDDDGE IEGLF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z35953 Genomic DNA. Translation: CAA85029.1.
J03724 Genomic DNA. Translation: AAA34781.1.
BK006936 Genomic DNA. Translation: DAA07203.1.
PIRA28174.
RefSeqNP_009640.1. NM_001178432.1.

3D structure databases

ProteinModelPortalP09440.
SMRP09440. Positions 37-326, 344-975.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32788. 95 interactions.
DIPDIP-6724N.
IntActP09440. 50 interactions.
MINTMINT-660665.
STRING4932.YBR084W.

Proteomic databases

PaxDbP09440.
PeptideAtlasP09440.
PRIDEP09440.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR084W; YBR084W; YBR084W.
GeneID852378.
KEGGsce:YBR084W.

Organism-specific databases

CYGDYBR084w.
SGDS000000288. MIS1.

Phylogenomic databases

eggNOGCOG0190.
GeneTreeENSGT00750000117947.
HOGENOMHOG000040280.
KOK00288.
OMALPTHAGF.
OrthoDBEOG7K0ZMJ.

Enzyme and pathway databases

BioCycYEAST:YBR084W-MONOMER.
UniPathwayUPA00193.

Gene expression databases

GenevestigatorP09440.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPMF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProIPR000559. 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]
PfamPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSPR00085. THFDHDRGNASE.
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00721. 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]
ProtoNetSearch...

Other

NextBio971174.

Entry information

Entry nameC1TM_YEAST
AccessionPrimary (citable) accession number: P09440
Secondary accession number(s): D6VQ83
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways