O43007 (C1TM_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	ade9
ORF Names:	SPBC2G2.08

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	972 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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.3.
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 Reference proteome
Gene Ontology (GO)
Biological_process	10-formyltetrahydrofolate biosynthetic process Inferred from sequence or structural similarity. Source: PomBase folic acid biosynthetic process Inferred from sequence orthology. Source: PomBase histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW purine nucleobase biosynthetic process Inferred from sequence orthology. Source: PomBase purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate interconversion Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrion Inferred from direct assay Ref.3. Source: PomBase
Molecular_function	ATP binding Inferred from sequence model. Source: PomBase formate-tetrahydrofolate ligase activity Inferred from sequence or structural similarity. Source: PomBase methenyltetrahydrofolate cyclohydrolase activity Inferred from sequence or structural similarity. Source: PomBase methylenetetrahydrofolate dehydrogenase (NADP+) activity Inferred from sequence or structural similarity. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 55	55	Mitochondrion Potential
	Chain	56 – 972	917	C-1-tetrahydrofolate synthase, mitochondrial		PRO_0000315627
Regions
	Nucleotide binding	202 – 204	3	NADP By similarity
	Nucleotide binding	405 – 412	8	ATP By similarity
	Region	56 – 340	285	Methylenetetrahydrofolate dehydrogenase and cyclohydrolase
	Region	84 – 88	5	Substrate binding By similarity
	Region	131 – 133	3	Substrate binding By similarity
	Region	299 – 303	5	Substrate binding By similarity
	Region	341 – 972	632	Formyltetrahydrofolate synthetase
Sites
	Binding site	227	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	O43007 [UniParc]. Last modified October 3, 2012. Version 3. Checksum: A14DFE32C0106F20	FASTA	972	105,757
	10 20 30 40 50 60 MNVMVSFNQL RNYFLESNSL RPSKWLFQSY GTSSSANILN GKLLARKLQR SVAEEVQALK 70 80 90 100 110 120 AKDRNFKPAL AIVQVGKRED SNVYVRMKEK AARLVGIDFK YCPFPETIQM PALLHELKKL 130 140 150 160 170 180 NDDHTVHGVL VQLPLPKHLN ERTVTESITP PKDVDGFGAF NIGLLAKNDA TPIHYPCTPK 190 200 210 220 230 240 GIMELLKDNK ISVAGLNAVV LGRSDIVGNP ISYLLRKDNA TVTVCHSKTK DLIQHISNAD 250 260 270 280 290 300 LVIAALGKPE FVRGEWLKPG SVVVDVGINA VQRNGKRVLV GDVHFESASK VASSITPVPG 310 320 330 340 350 360 GVGPMTVAML MENIVNAAKI ARTENIYRKI DLNPLELKKP VPSDIEIANS QEPKLISNLA 370 380 390 400 410 420 KEMGIYDTEL ENYGNYKAKV NLAVYERLKH RKDGNYVVVS GITPTPFGEG KSTVVAGLVQ 430 440 450 460 470 480 AMGHLGKLGI ACVRQPSQGP TFGVKGGAAG GGYAQFIPMD DFNLHMTGDI HAVTAANNLL 490 500 510 520 530 540 VAALETRMFH ENTQSDAALI KRLIPVKNGR RVIPRGLIGR WNRICASHNM DPEDVNNASP 550 560 570 580 590 600 ELLKEFVRLN VDPDTIECNR VLDVNDRFLR SIEVGKASTE KGHVRKTSFD ISVASECMSI 610 620 630 640 650 660 LALSCDLNDM HSRLSRMVIA NDKYGNAITA GDLGVSGALT VLLKDAIKPN LMQTLEGTPA 670 680 690 700 710 720 FVHAGPFANI SIGASSIIAD KIALKLAGTE SFDRPEDAGY VVTEAGFASD MGMEKFFNIK 730 740 750 760 770 780 CRYSKLVPNT VVLVTTVKAL KLHGGGPKLK PGAPIPEEYL VENLDLVKNG CSNMVKHIQN 790 800 810 820 830 840 CHKFNIPVVV AINSYKTDSS KEHEIIREAA LQAGAVDAVP SDHWAQGGKG AIELAKSVMT 850 860 870 880 890 900 ACDQSSNSKF RLLYDSETSI EDKVNVIAKE MYGANGVEFS SLAKERINTF IKQGFGNLPI 910 920 930 940 950 960 CMAKTQYSLS HNPEFRNVPK NFTVPIRDMR LNAGAGFIYP LAAEIQTIPG LPTAPAYLNI 970 DICENGEIVG LS

References

	« Hide 'large scale' referencesShow 'large scale' 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Comparative functional genomics of the fission yeasts." Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K. , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C. Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVISION OF GENE MODEL.
[3]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA17888.3.
PIR	T40147.
RefSeq	NP_596437.2. NM_001022356.2.
3D structure databases
HSSP	HSSP built from PDB template 1A4I based on UniProtKB P11586.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPBC2G2.08-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2540300.
KEGG	spo:SPBC2G2.08.
Organism-specific databases
PomBase	SPBC2G2.08.
Phylogenomic databases
eggNOG	COG0190.
HOGENOM	HOG000040280.
KO	K00288.
OrthoDB	EOG4TF3TC.
Enzyme and pathway databases
UniPathway	UPA00193.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
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]
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...
Other
NextBio	20801430.

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:	October 3, 2012
Last modified:	May 1, 2013
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program