Reviewed, UniProtKB/Swiss-Prot O43007 (C1TM_SCHPO)

Names and origin

Protein names

Recommended name:
    C-1-tetrahydrofolate synthase, mitochondrial
      Short name=C1-THF synthase
Including the following 3 domains:
    1- Recommended name:
            Methylenetetrahydrofolate dehydrogenase
              EC=1.5.1.5
    2- Recommended name:
            Methenyltetrahydrofolate cyclohydrolase
              EC=3.5.4.9
    3- Recommended name:
            Formyltetrahydrofolate synthetase
              EC=6.3.4.3

Gene names

Name:	ade9
ORF Names:	SPBC2G2.08

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	969 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH. 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.
Pathway	One-carbon metabolism; tetrahydrofolate interconversion.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion Ref.2.
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.
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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis Methionine biosynthesis One-carbon metabolism Purine biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding NADP Nucleotide-binding
Molecular function	Hydrolase Ligase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	folic acid and derivative biosynthetic process Inferred from electronic annotation. Source: InterPro histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW formate-tetrahydrofolate ligase activity Inferred from electronic annotation. Source: EC methenyltetrahydrofolate cyclohydrolase activity Inferred from electronic annotation. Source: EC methylenetetrahydrofolate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 52	52	Mitochondrion Potential
	Chain	53 – 969	917	C-1-tetrahydrofolate synthase, mitochondrial		PRO_0000315627
Regions
	Nucleotide binding	199 – 201	3	NADP By similarity
	Nucleotide binding	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
Sites
	Binding site	224	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	O43007-1 [UniParc]. Last modified November 1, 1999. Version 2. Checksum: DC8C3FF5B14D4C68	FASTA	969	105,412
	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

References

[1]

"The genome sequence of Schizosaccharomyces pombe." 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. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA17888.2.
PIR	T40147.
RefSeq	NP_596437.1.
3D structure databases
HSSP	HSSP built from PDB template 1A4I based on UniProtKB P11586.
SMR	O43007. Positions 32-319, 341-967.
ModBase	Search...
Protein-protein interaction databases
STRING	O43007.
Genome annotation databases
GeneID	2540300.
GenomeReviews	Gene locus ade9 in contig CU329671_GR.
KEGG	spo:SPBC2G2.08.
NMPDR	fig|4896.1.peg.2303.
Organism-specific databases
GeneDB_Spombe	SPBC2G2.08.
Phylogenomic databases
eggNOG	fuNOG04962.
HOGENOM	HBG677721.
OrthoDB	EOG9PK3R8.
PhylomeDB	O43007.
Enzyme and pathway databases
BRENDA	1.5.1.5. 653. 3.5.4.9. 653. 6.3.4.3. 653.
Gene expression databases
ArrayExpress	O43007.
Family and domain databases
InterPro	IPR000559. Formate_THF_ligase. IPR020628. Formate_THF_ligase_CS. IPR016040. NAD(P)-bd_dom. IPR000672. THF_DH/CycHdrlase. IPR020630. THF_DH/CycHdrlase_cat_dom. IPR020867. THF_DH/CycHdrlase_CS. IPR020631. THF_DH/CycHdrlase_NAD-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF01268. FTHFS. 1 hit. PF00763. THF_DHG_CYH. 1 hit. PF02882. THF_DHG_CYH_C. 1 hit. [Graphical view]
PRINTS	PR00085. THFDHDRGNASE.
PROSITE	PS00721. FTHFS_1. 1 hit. PS00767. THF_DHG_CYH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C1TM_SCHPO

Accession

Primary (citable) accession number: O43007

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 1, 1999
Last modified:	January 19, 2010
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)