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O96553

- C1TC_DROME

UniProt

O96553 - C1TC_DROME

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Protein

C-1-tetrahydrofolate synthase, cytoplasmic

Gene

pug

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH.By similarity
5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.By similarity
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei230 – 2301NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi205 – 2073NADPBy similarity
Nucleotide bindingi413 – 4208ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. formate-tetrahydrofolate ligase activity Source: UniProtKB
  3. methenyltetrahydrofolate cyclohydrolase activity Source: UniProtKB
  4. methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: UniProtKB

GO - Biological processi

  1. cellular amino acid biosynthetic process Source: UniProtKB
  2. folic acid-containing compound biosynthetic process Source: InterPro
  3. histidine biosynthetic process Source: UniProtKB-KW
  4. methionine biosynthetic process Source: UniProtKB-KW
  5. one-carbon metabolic process Source: RefGenome
  6. purine nucleotide biosynthetic process Source: UniProtKB-KW
  7. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis, Methionine biosynthesis, One-carbon metabolism, Purine biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_260373. Metabolism of folate and pterines.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
C-1-tetrahydrofolate synthase, cytoplasmic
Short name:
C1-THF synthase
Including the following 3 domains:
Methylenetetrahydrofolate dehydrogenase (EC:1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase (EC:3.5.4.9)
Formyltetrahydrofolate synthetase (EC:6.3.4.3)
Gene namesi
Name:pug
ORF Names:CG4067
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0020385. pug.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: RefGenome
  3. lipid particle Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 968968C-1-tetrahydrofolate synthase, cytoplasmicPRO_0000199324Add
BLAST

Proteomic databases

PaxDbiO96553.
PRIDEiO96553.

Expressioni

Tissue specificityi

Present in all tissues.1 Publication

Gene expression databases

BgeeiO96553.
ExpressionAtlasiO96553. differential.

Interactioni

Subunit structurei

Homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Keap1Q9VEN51EBI-118733,EBI-181742

Protein-protein interaction databases

BioGridi66423. 2 interactions.
IntActiO96553. 1 interaction.
MINTiMINT-297603.

Structurei

3D structure databases

ProteinModelPortaliO96553.
SMRiO96553. Positions 38-329, 350-968.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 338338Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseAdd
BLAST
Regioni86 – 905Substrate bindingBy similarity
Regioni133 – 1353Substrate bindingBy similarity
Regioni305 – 3095Substrate bindingBy similarity
Regioni339 – 968630Formyltetrahydrofolate synthetaseAdd
BLAST

Domaini

This trifunctional enzyme consists of two major domains: a N-terminal part, containing the methylene-THF dehydrogenase and the methenyl-THF cyclohydrolase activities and a larger formyl-THF synthetase domain.

Sequence similaritiesi

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.Curated
In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.Curated

Phylogenomic databases

eggNOGiCOG0190.
GeneTreeiENSGT00750000117401.
InParanoidiO96553.
KOiK00288.
OMAiFAPLMFK.
OrthoDBiEOG76T9QN.
PhylomeDBiO96553.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPiMF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProiIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamiPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform B (identifier: O96553-1) [UniParc]FASTAAdd to Basket

Also known as: D

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSAQYQRFLK VLEKWPAEKS KVGSGEWTAE PAIKMSGAKI ISGTAVAKSI
60 70 80 90 100
REELRNEVTA MSKQLADFVP GLRIVQVGGR EDSNVYIRMK IKAATEIGID
110 120 130 140 150
AAHVQLPRSI TEVELLDKIN DLNEDPRVHG IIVQMPLDCD TPIDSHRITD
160 170 180 190 200
AVSPEKDVDG LHTVNEGRLA IGDLGGFLPC TPWGCLELIR RSGVEIAGAR
210 220 230 240 250
AVVLGRSKIV GTPAAELLKW ANATVTVCHS KTRNLEEITR SADILVVGIG
260 270 280 290 300
VAEMVKGSWI KPGAVVIDCG INVKPDASKA SGSKLVGDVD YAEALQVAGH
310 320 330 340 350
LTPVPGGVGP MTVAMLMKNT VRSAARFLER LAKSQWALQT LPLKPQRPVP
360 370 380 390 400
SDIVIARAQK PKDIAVLAKE IGLEAREVSL YGNKKAKISL SVLERLKDKE
410 420 430 440 450
VGHYVVVAGM TPTPLGEGKT TTLMGLVQAL GAHKLRNTMA ALRQPSQGPT
460 470 480 490 500
FGIKGGAAGG GYAQVIPMEE FNLHLTGDIH AVSAANNLLA AQLDTRIFHE
510 520 530 540 550
NTQKDKALYD RLVPAIKGQR KFSPIQLRRL QKLGITKTDP DTLTADEYGP
560 570 580 590 600
FARLDIDPDT IMWERVVDIN DRYLRTITVG QSPTEKGISR ETRFSISVAS
610 620 630 640 650
EIMAVLALSR SLEDMKQRLA DMVVAFDKRG KPVTADDLGV TGALAVLLKD
660 670 680 690 700
ALEPNLMQSL EGTPVLVHAG PFANIAHGCN SIIADEVGLK LVGKNGFVCT
710 720 730 740 750
EAGFGSDIGM EKFCNIKCRT SGRKPNAMVL VATVRAIKMH GGGAPVTPGA
760 770 780 790 800
PLNKQYTEEN LELVQKGLPN LLQHIENGKA FGMPVVVSLN AHSADTPAEH
810 820 830 840 850
ELVKKAALEA GAFAAVVSTH WADGGAGAVQ LADAVIKACE QGNQFRLLYD
860 870 880 890 900
LELPLVDKMN KIATTMYGAG KVVLSPAAEE KVKRLTDAGF GNLPICMSKV
910 920 930 940 950
SGSFTGDAKI KGAPKGFTLD VEDVYVSAGA GFVVAMCGEV TKMPGLPTRP
960
AIYDIDLNTE TGEIEGLF

Note: No experimental confirmation available.

Length:968
Mass (Da):103,504
Last modified:July 19, 2004 - v4
Checksum:iD65EC8455DD8AF2C
GO
Isoform A (identifier: O96553-2) [UniParc]FASTAAdd to Basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Show »
Length:934
Mass (Da):99,627
Checksum:i42CC88A69A4D5345
GO

Sequence cautioni

The sequence AAL39291.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti879 – 8791E → K in AAX33426. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434Missing in isoform A. 1 PublicationVSP_010883Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF082097 Genomic DNA. Translation: AAC78847.1.
AE014297 Genomic DNA. Translation: AAG22140.2.
AE014297 Genomic DNA. Translation: AAN13478.1.
AE014297 Genomic DNA. Translation: AAN13479.1.
AE014297 Genomic DNA. Translation: AAX52944.1.
BT021278 mRNA. Translation: AAX33426.1.
AY069146 mRNA. Translation: AAL39291.1. Different initiation.
RefSeqiNP_001014614.1. NM_001014614.2. [O96553-1]
NP_477254.1. NM_057906.4. [O96553-2]
NP_731489.2. NM_169350.3. [O96553-1]
NP_731490.1. NM_169351.2. [O96553-2]
UniGeneiDm.14326.

Genome annotation databases

EnsemblMetazoaiFBtr0082264; FBpp0081741; FBgn0020385. [O96553-1]
FBtr0100144; FBpp0099494; FBgn0020385. [O96553-1]
GeneIDi41279.
KEGGidme:Dmel_CG4067.
UCSCiCG4067-RA. d. melanogaster. [O96553-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF082097 Genomic DNA. Translation: AAC78847.1 .
AE014297 Genomic DNA. Translation: AAG22140.2 .
AE014297 Genomic DNA. Translation: AAN13478.1 .
AE014297 Genomic DNA. Translation: AAN13479.1 .
AE014297 Genomic DNA. Translation: AAX52944.1 .
BT021278 mRNA. Translation: AAX33426.1 .
AY069146 mRNA. Translation: AAL39291.1 . Different initiation.
RefSeqi NP_001014614.1. NM_001014614.2. [O96553-1 ]
NP_477254.1. NM_057906.4. [O96553-2 ]
NP_731489.2. NM_169350.3. [O96553-1 ]
NP_731490.1. NM_169351.2. [O96553-2 ]
UniGenei Dm.14326.

3D structure databases

ProteinModelPortali O96553.
SMRi O96553. Positions 38-329, 350-968.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 66423. 2 interactions.
IntActi O96553. 1 interaction.
MINTi MINT-297603.

Proteomic databases

PaxDbi O96553.
PRIDEi O96553.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0082264 ; FBpp0081741 ; FBgn0020385 . [O96553-1 ]
FBtr0100144 ; FBpp0099494 ; FBgn0020385 . [O96553-1 ]
GeneIDi 41279.
KEGGi dme:Dmel_CG4067.
UCSCi CG4067-RA. d. melanogaster. [O96553-1 ]

Organism-specific databases

CTDi 41279.
FlyBasei FBgn0020385. pug.

Phylogenomic databases

eggNOGi COG0190.
GeneTreei ENSGT00750000117401.
InParanoidi O96553.
KOi K00288.
OMAi FAPLMFK.
OrthoDBi EOG76T9QN.
PhylomeDBi O96553.

Enzyme and pathway databases

UniPathwayi UPA00193 .
Reactomei REACT_260373. Metabolism of folate and pterines.

Miscellaneous databases

GenomeRNAii 41279.
NextBioi 823064.
PROi O96553.

Gene expression databases

Bgeei O96553.
ExpressionAtlasi O96553. differential.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPi MF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProi IPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020867. THF_DH/CycHdrlase_CS.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view ]
Pfami PF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view ]
PRINTSi PR00085. THFDHDRGNASE.
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
PS00766. THF_DHG_CYH_1. 1 hit.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Dominant defects in Drosophila eye pigmentation resulting from a euchromatin-heterochromatin fusion gene."
    Rong Y.S., Golic K.G.
    Genetics 150:1551-1566(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Embryo.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 604-968.
    Strain: Berkeley1 Publication.
    Tissue: Head1 Publication.

Entry informationi

Entry nameiC1TC_DROME
AccessioniPrimary (citable) accession number: O96553
Secondary accession number(s): A4V2N7
, A4V2N9, Q5BIE6, Q8T0P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: July 19, 2004
Last modified: November 26, 2014
This is version 112 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3