Reviewed, UniProtKB/Swiss-Prot Q8WZJ7 (C1TC_SCHPO)

Names and origin

Protein names

Recommended name:
    C-1-tetrahydrofolate synthase, cytoplasmic
      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

ORF Names:

SPBC839.16

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	937 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	5,10-methylenetetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH. 5,10-methenyltetrahydrofolate + H(2)O = 10-formyltetrahydrofolate. ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.
Pathway	One-carbon metabolism; tetrahydrofolate pathway.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm.
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	Cytoplasm
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 compound 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	cytosol Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro formate-tetrahydrofolate ligase activity Inferred from electronic annotation. Source: InterPro 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
	Chain	1 – 937	937	C-1-tetrahydrofolate synthase, cytoplasmic		PRO_0000315626
Regions
	Nucleotide binding	168 – 170	3	NADP By similarity
	Nucleotide binding	374 – 381	8	ATP By similarity
	Region	1 – 309	309	Methylenetetrahydrofolate dehydrogenase and cyclohydrolase
	Region	50 – 54	5	Substrate binding By similarity
	Region	97 – 99	3	Substrate binding By similarity
	Region	268 – 272	5	Substrate binding By similarity
	Region	310 – 937	628	Formyltetrahydrofolate synthetase
Sites
	Binding site	193	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8WZJ7-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 70FF8700FD023C90	FASTA	937	101,203
	10 20 30 40 50 60 MALLLEGTSL ARKVREELRE QISSIKSVDP YFNVSLKIIQ VGGREDSNVY VRMKTRAANE 70 80 90 100 110 120 AGISCEHVNF PEDITEYDLL LAIKGFNEDP TVHGIIVQLP LPAHINEQII TEAVAPEKDV 130 140 150 160 170 180 DGFCETNLGK LTKREGQPLF TACTPKGIMC ILKHYGINVQ GKHAVVIGRS NIVGRPMSIL 190 200 210 220 230 240 LEKANATVTL CHSKTESIAD IVRTADIVVA AIGIPHFVKA DWLKKGVVAI DVGINSIPDA 250 260 270 280 290 300 TKKSGYRLTG DIDFENAKEV ASAITPVPGS VGPMTVAMLL QNVVESAVRF RKMSRKRKPT 310 320 330 340 350 360 LLPLKLQTPV PSDIEIARSQ TPKNIGDLAS EIGIAKSELE FYGSHKAKVN LEILQRLAHR 370 380 390 400 410 420 RDGHYVVVTG ITPTPFGEGK STLTAGLVQA LSNLDKLAIA CVRQPSQGPT FGIKGGAAGG 430 440 450 460 470 480 GYSQFIPMEE FNLHLTGDIH AITAATNLLA AAIDTRMFHE NTQSDAALYK RLTLVKGNKR 490 500 510 520 530 540 EFAPVMFRRL KKLGIDKTNP EELTEEEQRK FARLDIEPST ISWNRTLDVN DRFLRKITIG 550 560 570 580 590 600 ENPTEKGFTR QTGFDLSVAS ECMSVLALAT DLKDMRERLG RMVVASNKSG EPVTADDLGV 610 620 630 640 650 660 GGALTVLLKD AIKPTLMQTL EGTPALVHAG PFANISIGAS SILADRIALK LAGTEVDEDA 670 680 690 700 710 720 KKEAGYVVTE AGFASDIGME KFFNIKCRTS GLKPDAIVIV ATVQALKLHG GGPPVGPGKP 730 740 750 760 770 780 IPEVYKREDV DLVRKGCANL AKHISNARKY GLPVVVAINK FSSDSPNEIS AIREEALAAG 790 800 810 820 830 840 ATDAVDSNHW AEGGKGALGV ARALINACEN VDSEFRLLYD VHEPIEKKIE IIAKEMYGAD 850 860 870 880 890 900 GIELSPLAKE RLETFTKQGY NNLPICIAKT QYSLSHDPDL KGAPTNFTVP IRDMRLSAGA 910 920 930 GFIYPLAAAI STIPGLPTKP AYYNIDIAEN GDIVGLS

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
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAB46709.1.
PIR	T40723.
RefSeq	NP_595256.1.
3D structure databases
HSSP	HSSP built from PDB template 1A4I based on UniProtKB P11586.
ModBase	Search...
Genome annotation databases
GeneID	2541217.
KEGG	spo:SPBC839.16.
NMPDR	fig|4896.1.peg.1122.
Organism-specific databases
GeneDB_Spombe	SPBC839.16.
Gene expression databases
ArrayExpress	Q8WZJ7.
Family and domain databases
InterPro	IPR000559. Fmtethyd_synth. IPR016040. NAD(P)-bd. IPR000672. THF_DHase/CycOHase. [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.
ProDom	PD002300. THFDhg/Cyc_hydro. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00721. FTHFS_1. 1 hit. PS00722. FTHFS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C1TC_SCHPO

Accession

Primary (citable) accession number: Q8WZJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 1, 2002
Last modified:	November 25, 2008
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)