Methylenetetrahydrofolate dehydrogenase
     (EC 1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase
     (EC 3.5.4.9)
Formyltetrahydrofolate synthetase
     (EC 6.3.4.3)

Gene name

	Name:	ade9
	ORFNames:	SPBC2G2.08

From

Schizosaccharomyces pombe (Fission yeast)

[TaxID: 4896]

Taxonomy

Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.

Protein existence

2: Evidence at transcript level;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).

[2]

SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nbt1222; PubMed=16823372 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).

Comments

CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NADP⁺ = 5,10-methenyltetrahydrofolate + NADPH.
CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H₂O = 10-formyltetrahydrofolate.
CATALYTIC ACTIVITY: ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.
PATHWAY: One-carbon metabolism; tetrahydrofolate pathway .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Mitochondrion.
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.
SIMILARITY: In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
SIMILARITY: In the C-terminal section; belongs to the formate--tetrahydrofolate ligase 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

CU329671; CAA17888.2; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T40147; T40147.

RefSeq

NP_596437.1; -.

3D structure databases

HSSP

P11586; 1A4I. [HSSP ENTRY / PDB]

ModBase

O43007.

Organism-specific databases

GeneDB_Spombe

SPBC2G2.08; -.

Gene expression databases

ArrayExpress

O43007; -.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004329;	Molecular function: formate-tetrahydrofolate ligase activity (inferred from electronic annotation from InterPro).
GO:0004477;	Molecular function: methenyltetrahydrofolate cyclohydrolase activity (inferred from electronic annotation from EC).
GO:0004488;	Molecular function: methylenetetrahydrofolate dehydrogenase (NADP+) activity (inferred from electronic annotation from EC).
GO:0009396;	Biological process: folic acid and derivative biosynthetic process (inferred from electronic annotation from InterPro).
GO:0000105;	Biological process: histidine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0009086;	Biological process: methionine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006730;	Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006164;	Biological process: purine nucleotide biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000559; Fmtethyd_synth.
IPR016040; NAD(P)-bd.
IPR000672; THF_DHase/CycOHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF01268; FTHFS; 1.
PF00763; THF_DHG_CYH; 1.
PF02882; THF_DHG_CYH_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00085; THFDHDRGNASE.

ProDom

PD002300; THFDhg/Cyc_hydro; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00721; FTHFS_1; 1.
PS00767; THF_DHG_CYH_2; 1.

Genome annotation databases

GeneID

2540300; -.

KEGG

spo:SPBC2G2.08; -.

NMPDR

fig|4896.1.peg.2303; -.

Other

ProtoNet

O43007.

UniRef

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

Keywords

Amino-acid biosynthesis; ATP-binding; Complete proteome; Histidine biosynthesis; Hydrolase; Ligase; Methionine biosynthesis; Mitochondrion; Multifunctional enzyme; NADP; Nucleotide-binding; One-carbon metabolism; Oxidoreductase; Purine biosynthesis; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 52`	`52`	`Mitochondrion (Potential).`
`CHAIN`	`53 969`	`917`	`C-1-tetrahydrofolate synthase, mitochondrial.`	`PRO_0000315627`
`NP_BIND`	`199 201`	`3`	`NADP (By similarity).`
`NP_BIND`	`402 409`	`8`	`ATP (By similarity).`
`REGION`	`53 337`	`285`	`Methylenetetrahydrofolate dehydrogenase and cyclohydrolase.`
`REGION`	`81 85`	`5`	`Substrate binding (By similarity).`
`REGION`	`128 130`	`3`	`Substrate binding (By similarity).`
`REGION`	`296 300`	`5`	`Substrate binding (By similarity).`
`REGION`	`338 969`	`632`	`Formyltetrahydrofolate synthetase.`
`BINDING`	`224 224`		`NADP (By similarity).`

Sequence information

Length: 969 AA [This is the length of the unprocessed precursor]

Molecular weight: 105412 Da [This is the MW of the unprocessed precursor]

CRC64: DC8C3FF5B14D4C68 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVSFNQLRNY FLESNSLRPS KWLFQSYGTS SSANILNGKL LARKLQRSVA EEVQALKAKD 

        70         80         90        100        110        120 
RNFKPALAIV QVGKREDSNV YVRMKEKAAR LVGIDFKYCP FPETIQMPAL LHELKKLNDD 

       130        140        150        160        170        180 
HTVHGVLVQL PLPKHLNERT VTESITPPKD VDGFGAFNIG LLAKNDATPI HYPCTPKGIM 

       190        200        210        220        230        240 
ELLKDNKISV AGLNAVVLGR SDIVGNPISY LLRKDNATVT VCHSKTKDLI QHISNADLVI 

       250        260        270        280        290        300 
AALGKPEFVR GEWLKPGSVV VDVGINAVQR NGKRVLVGDV HFESASKVAS SITPVPGGVG 

       310        320        330        340        350        360 
PMTVAMLMEN IVNAAKIART ENIYRKIDLN PLELKKPVPS DIEIANSQEP KLISNLAKEM 

       370        380        390        400        410        420 
GIYDTELENY GNYKAKVNLA VYERLKHRKD GNYVVVSGIT PTPFGEGKST VVAGLVQAMG 

       430        440        450        460        470        480 
HLGKLGIACV RQPSQGPTFG VKGGAAGGGY AQFIPMDDFN LHMTGDIHAV TAANNLLVAA 

       490        500        510        520        530        540 
LETRMFHENT QSDAALIKRL IPVKNGRRVI PRGLIGRWNR ICASHNMDPE DVNNASPELL 

       550        560        570        580        590        600 
KEFVRLNVDP DTIECNRVLD VNDRFLRSIE VGKASTEKGH VRKTSFDISV ASECMSILAL 

       610        620        630        640        650        660 
SCDLNDMHSR LSRMVIANDK YGNAITAGDL GVSGALTVLL KDAIKPNLMQ TLEGTPAFVH 

       670        680        690        700        710        720 
AGPFANISIG ASSIIADKIA LKLAGTESFD RPEDAGYVVT EAGFASDMGM EKFFNIKCRY 

       730        740        750        760        770        780 
SKLVPNTVVL VTTVKALKLH GGGPKLKPGA PIPEEYLVEN LDLVKNGCSN MVKHIQNCHK 

       790        800        810        820        830        840 
FNIPVVVAIN SYKTDSSKEH EIIREAALQA GAVDAVPSDH WAQGGKGAIE LAKSVMTACD 

       850        860        870        880        890        900 
QSSNSKFRLL YDSETSIEDK VNVIAKEMYG ANGVEFSSLA KERINTFIKQ GFGNLPICMA 

       910        920        930        940        950        960 
KTQYSLSHNP EFRNVPKNFT VPIRDMRLNA GAGFIYPLAA EIQTIPGLPT APAYLNIDIC 


ENGEIVGLS

O43007 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