ID C1TM_SCHPO Reviewed; 969 AA. AC O43007; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 2. DT 16-JUN-2009, entry version 46. DE RecName: Full=C-1-tetrahydrofolate synthase, mitochondrial; DE Short=C1-THF synthase; DE Includes: DE RecName: Full=Methylenetetrahydrofolate dehydrogenase; DE EC=1.5.1.5; DE Includes: DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase; DE EC=3.5.4.9; DE Includes: DE RecName: Full=Formyltetrahydrofolate synthetase; DE EC=6.3.4.3; DE Flags: Precursor; GN Name=ade9; ORFNames=SPBC2G2.08; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=16823372; DOI=10.1038/nbt1222; RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., RA Yoshida M.; RT "ORFeome cloning and global analysis of protein localization in the RT fission yeast Schizosaccharomyces pombe."; RL Nat. Biotechnol. 24:841-847(2006). CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NADP(+) = CC 5,10-methenyltetrahydrofolate + NADPH. CC -!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10- CC formyltetrahydrofolate. CC -!- CATALYTIC ACTIVITY: ATP + formate + tetrahydrofolate = ADP + CC phosphate + 10-formyltetrahydrofolate. CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate pathway. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- DOMAIN: This trifunctional enzyme consists of two major domains: CC an N-terminal part containing the methylene-THF dehydrogenase and CC cyclohydrolase activities and a larger C-terminal part containing CC formyl-THF synthetase activity. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC tetrahydrofolate dehydrogenase/cyclohydrolase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the formate-- CC tetrahydrofolate ligase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU329671; CAA17888.2; -; Genomic_DNA. DR PIR; T40147; T40147. DR RefSeq; NP_596437.1; -. DR HSSP; P11586; 1A4I. DR GeneID; 2540300; -. DR KEGG; spo:SPBC2G2.08; -. DR NMPDR; fig|4896.1.peg.2303; -. DR GeneDB_Spombe; SPBC2G2.08; -. DR BRENDA; 1.5.1.5; 653. DR BRENDA; 3.5.4.9; 653. DR BRENDA; 6.3.4.3; 653. DR ArrayExpress; O43007; -. DR GO; GO:0005739; C:mitochondrion; IDA:GeneDB_SPombe. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:EC. DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase act...; IEA:EC. DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NA...; IEA:EC. DR GO; GO:0009396; P:folic acid and derivative biosynthetic process; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006730; P:one-carbon compound metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR000559; For_THF_ligase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000672; THF_DH/CycHdrlase. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF01268; FTHFS; 1. DR Pfam; PF00763; THF_DHG_CYH; 1. DR Pfam; PF02882; THF_DHG_CYH_C; 1. DR PRINTS; PR00085; THFDHDRGNASE. DR ProDom; PD002300; THFDhg/Cyc_hydro; 1. DR PROSITE; PS00721; FTHFS_1; 1. DR PROSITE; PS00767; THF_DHG_CYH_2; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; KW Histidine biosynthesis; Hydrolase; Ligase; Methionine biosynthesis; KW Mitochondrion; Multifunctional enzyme; NADP; Nucleotide-binding; KW One-carbon metabolism; Oxidoreductase; Purine biosynthesis; KW Transit peptide. FT TRANSIT 1 52 Mitochondrion (Potential). FT CHAIN 53 969 C-1-tetrahydrofolate synthase, FT mitochondrial. FT /FTId=PRO_0000315627. FT NP_BIND 199 201 NADP (By similarity). FT NP_BIND 402 409 ATP (By similarity). FT REGION 53 337 Methylenetetrahydrofolate dehydrogenase FT and cyclohydrolase. FT REGION 81 85 Substrate binding (By similarity). FT REGION 128 130 Substrate binding (By similarity). FT REGION 296 300 Substrate binding (By similarity). FT REGION 338 969 Formyltetrahydrofolate synthetase. FT BINDING 224 224 NADP (By similarity). SQ SEQUENCE 969 AA; 105412 MW; DC8C3FF5B14D4C68 CRC64; MVSFNQLRNY FLESNSLRPS KWLFQSYGTS SSANILNGKL LARKLQRSVA EEVQALKAKD RNFKPALAIV QVGKREDSNV YVRMKEKAAR LVGIDFKYCP FPETIQMPAL LHELKKLNDD HTVHGVLVQL PLPKHLNERT VTESITPPKD VDGFGAFNIG LLAKNDATPI HYPCTPKGIM ELLKDNKISV AGLNAVVLGR SDIVGNPISY LLRKDNATVT VCHSKTKDLI QHISNADLVI AALGKPEFVR GEWLKPGSVV VDVGINAVQR NGKRVLVGDV HFESASKVAS SITPVPGGVG PMTVAMLMEN IVNAAKIART ENIYRKIDLN PLELKKPVPS DIEIANSQEP KLISNLAKEM GIYDTELENY GNYKAKVNLA VYERLKHRKD GNYVVVSGIT PTPFGEGKST VVAGLVQAMG HLGKLGIACV RQPSQGPTFG VKGGAAGGGY AQFIPMDDFN LHMTGDIHAV TAANNLLVAA LETRMFHENT QSDAALIKRL IPVKNGRRVI PRGLIGRWNR ICASHNMDPE DVNNASPELL KEFVRLNVDP DTIECNRVLD VNDRFLRSIE VGKASTEKGH VRKTSFDISV ASECMSILAL SCDLNDMHSR LSRMVIANDK YGNAITAGDL GVSGALTVLL KDAIKPNLMQ TLEGTPAFVH AGPFANISIG ASSIIADKIA LKLAGTESFD RPEDAGYVVT EAGFASDMGM EKFFNIKCRY SKLVPNTVVL VTTVKALKLH GGGPKLKPGA PIPEEYLVEN LDLVKNGCSN MVKHIQNCHK FNIPVVVAIN SYKTDSSKEH EIIREAALQA GAVDAVPSDH WAQGGKGAIE LAKSVMTACD QSSNSKFRLL YDSETSIEDK VNVIAKEMYG ANGVEFSSLA KERINTFIKQ GFGNLPICMA KTQYSLSHNP EFRNVPKNFT VPIRDMRLNA GAGFIYPLAA EIQTIPGLPT APAYLNIDIC ENGEIVGLS //