[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169872 [NCBI, ExPASy, EBI, Israel, Japan] Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; Nature 387:90-93(1997).
[2]	CHARACTERIZATION. DOI=10.1074/jbc.275.19.14056; PubMed=10799479 [NCBI, ExPASy, EBI, Israel, Japan] Cherest H., Thomas D., Surdin-Kerjan Y.; "Polyglutamylation of folate coenzymes is necessary for methionine biosynthesis and maintenance of intact mitochondrial genome in Saccharomyces cerevisiae."; J. Biol. Chem. 275:14056-14063(2000).
[3]	SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan] Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.; "Global analysis of protein localization in budding yeast."; Nature 425:686-691(2003).
[4]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).

Comments

FUNCTION: Conversion of folates to polyglutamate derivatives.
CATALYTIC ACTIVITY: ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).
PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: Present with 2340 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the folylpolyglutamate synthase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z49702; CAA89750.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S54574; S54574.

RefSeq

NP_013831.1; -.

3D structure databases

HSSP

P15925; 1FGS. [HSSP ENTRY / PDB]

ModBase

Q12676.

Organism-specific databases

YMR113w; -.

S000004719; FOL3.

Gene expression databases

ArrayExpress

Q12676; -.

GermOnline

YMR113W; Saccharomyces cerevisiae.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0008841;	Molecular function: dihydrofolate synthase activity (inferred from mutant phenotype from SGD).
GO:0004326;	Molecular function: tetrahydrofolylpolyglutamate synthase activity (inferred from electronic annotation from InterPro).
GO:0009396;	Biological process: folic acid and derivative biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006730;	Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001645; Fpolygl_synthtse.
IPR013221; Mur_ligase_cen.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.1190.10; Mur_ligase_cen; 1.

PANTHER

PTHR11136; Fpolygl_synthtse; 1.

Pfam

PF08245; Mur_ligase_M; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01499; folC; 1.

PROSITE

PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PS01012; FOLYLPOLYGLU_SYNT_2; 1.

ProtoNet

Q12676.

Genome annotation databases

Ensembl

YMR113W; Saccharomyces cerevisiae. [Contig view]

855140; -.

Z71257_GR; YMR113W.

sce:YMR113W; -.

fig|4932.3.peg.4879; -.

Phylogenomic databases

HOGENOM

Q12676; -.

Other

LinkHub

Q12676; -.

NextBio

978528; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; One-carbon metabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 427`	`427`	`Folylpolyglutamate synthase.`	`PRO_0000168308`
`NP_BIND`	`30 36`	`7`	`ATP (Potential).`

Sequence information

Length: 427 AA [This is the length of the unprocessed precursor]

Molecular weight: 47851 Da [This is the MW of the unprocessed precursor]

CRC64: C3307CEF43BE1F30 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAIELGLSRI TKLLEHLGNP QNSLRVLHIA GTNGKGSVCT YLSSVLQQKS YQIGKFTTPH 

        70         80         90        100        110        120 
LVHVTDSITI NNKPIPLERY QNIRLQLEAL NKSHSLKCTE FELLTCTAFK YFYDVQCQWC 

       130        140        150        160        170        180 
VIEVGLGGRL DATNVIPGAN KACCGITKIS LDHESFLGNT LSEISKEKAG IITEGVPFTV 

       190        200        210        220        230        240 
IDGTNEASVI NVVKERCKAL GSELSVTDSQ LNGNMIDTNS WGCFDLAKLP LNGEYQIFNL 

       250        260        270        280        290        300 
RVAMGMLDYL QMNELIDITK NEVSTRLAKV DWPGRLYRMD YRFDKVSNRT VPILMDGAHN 

       310        320        330        340        350        360 
GSAAVELVKY LRKEYGNQPL TFVMAVTHGK NLEPLLQPLL RPIDQVILTR FNNVEGMPWI 

       370        380        390        400        410        420 
HATDPEEIKD FILTQGYTKE IVIENDLHQV LPSLAHVSDE QRRPIVVCGS LYLCGELLRI 


HNSHLRN

Q12676 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools