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UniProtKB/Swiss-Prot entry O96553


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name C1TC_DROME
Primary accession number O96553
Secondary accession numbers A4V2N7 A4V2N9 Q5BIE6 Q8T0P2
Integrated into Swiss-Prot on September 19, 2003
Sequence was last modified on July 19, 2004 (Sequence version 4)
Annotations were last modified on    November 4, 2008 (Entry version 63)
Name and origin of the protein
Protein name C-1-tetrahydrofolate synthase, cytoplasmic
Synonym C1-THF synthase
Includes Methylenetetrahydrofolate dehydrogenase
     (EC 1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase
     (EC 3.5.4.9)
Formyltetrahydrofolate synthetase
     (EC 6.3.4.3)
Gene name
Name: pug
ORFNames: CG4067
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=9832531 [NCBI, ExPASy, EBI, Israel, Japan]
Rong Y.S., Golic K.G.;
"Dominant defects in Drosophila eye pigmentation resulting from a euchromatin-heterochromatin fusion gene.";
Genetics 150:1551-1566(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley;
TISSUE=Embryo;
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 604-968.
STRAIN=Berkeley;
TISSUE=Head;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF082097; AAC78847.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAG22140.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAN13478.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAN13479.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAX52944.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT021278; AAX33426.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY069146; AAL39291.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001014614.1; -.
NP_477254.1; -.
NP_731489.2; -.
NP_731490.1; -.
UniGene Dm.14326
3D structure databases
HSSP P11586; 1A4I. [HSSP ENTRY / PDB]
ModBase O96553.
Protein-protein interaction databases
IntAct O96553; -.
Organism-specific databases
FlyBase FBgn0020385; pug.
Gene expression databases
ArrayExpress O96553; -.
GermOnline CG4067; Drosophila melanogaster.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0004329; Molecular function: formate-tetrahydrofolate ligase activity (non-traceable author statement from UniProtKB).
GO:0004477; Molecular function: methenyltetrahydrofolate cyclohydrolase activity (non-traceable author statement from UniProtKB).
GO:0004488; Molecular function: methylenetetrahydrofolate dehydrogenase (NADP+) activity (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008652; Biological process: amino acid biosynthetic process (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000559; Fmtethyd_synth.
IPR016040; NAD(P)-bd.
IPR000672; THF_DHase/CycOHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF01268; FTHFS; 1.
PF00763; THF_DHG_CYH; 1.
PF02882; THF_DHG_CYH_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00085; THFDHDRGNASE.
ProDom PD002300; THFDhg/Cyc_hydro; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00721; FTHFS_1; 1.
PS00722; FTHFS_2; 1.
PS00766; THF_DHG_CYH_1; 1.
PS00767; THF_DHG_CYH_2; 1.
BLOCKS O96553.
ProtoNet O96553.
Genome annotation databases
Ensembl CG4067; Drosophila melanogaster. [Contig view]
GeneID 41279; -.
KEGG dme:Dmel_CG4067; -.
Phylogenomic databases
HOGENOM O96553; -.
Other
NextBio 823064; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; Histidine biosynthesis; Hydrolase; Ligase; Methionine biosynthesis; Multifunctional enzyme; NADP; Nucleotide-binding; One-carbon metabolism; Oxidoreductase; Purine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   968  968     C-1-tetrahydrofolate synthase, cytoplasmic. PRO_0000199324
NP_BIND   205   207  3     NADP (By similarity). 
NP_BIND   413   420  8     ATP (By similarity). 
REGION   1   338  338     Methylenetetrahydrofolate dehydrogenase and cyclohydrolase. 
REGION   86    90  5     Substrate binding (By similarity). 
REGION   133   135  3     Substrate binding (By similarity). 
REGION   305   309  5     Substrate binding (By similarity). 
REGION   339   968  630     Formyltetrahydrofolate synthetase. 
BINDING   230   230        NADP (By similarity). 
VAR_SEQ   1    34        Missing (in isoform A). VSP_010883
CONFLICT   879   879        E -> K (in Ref. 4; AAX33426). 
Sequence information
Length: 968 AA [This is the length of the unprocessed precursor] Molecular weight: 103504 Da [This is the MW of the unprocessed precursor] CRC64: D65EC8455DD8AF2C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSAQYQRFLK VLEKWPAEKS KVGSGEWTAE PAIKMSGAKI ISGTAVAKSI REELRNEVTA 

        70         80         90        100        110        120 
MSKQLADFVP GLRIVQVGGR EDSNVYIRMK IKAATEIGID AAHVQLPRSI TEVELLDKIN 

       130        140        150        160        170        180 
DLNEDPRVHG IIVQMPLDCD TPIDSHRITD AVSPEKDVDG LHTVNEGRLA IGDLGGFLPC 

       190        200        210        220        230        240 
TPWGCLELIR RSGVEIAGAR AVVLGRSKIV GTPAAELLKW ANATVTVCHS KTRNLEEITR 

       250        260        270        280        290        300 
SADILVVGIG VAEMVKGSWI KPGAVVIDCG INVKPDASKA SGSKLVGDVD YAEALQVAGH 

       310        320        330        340        350        360 
LTPVPGGVGP MTVAMLMKNT VRSAARFLER LAKSQWALQT LPLKPQRPVP SDIVIARAQK 

       370        380        390        400        410        420 
PKDIAVLAKE IGLEAREVSL YGNKKAKISL SVLERLKDKE VGHYVVVAGM TPTPLGEGKT 

       430        440        450        460        470        480 
TTLMGLVQAL GAHKLRNTMA ALRQPSQGPT FGIKGGAAGG GYAQVIPMEE FNLHLTGDIH 

       490        500        510        520        530        540 
AVSAANNLLA AQLDTRIFHE NTQKDKALYD RLVPAIKGQR KFSPIQLRRL QKLGITKTDP 

       550        560        570        580        590        600 
DTLTADEYGP FARLDIDPDT IMWERVVDIN DRYLRTITVG QSPTEKGISR ETRFSISVAS 

       610        620        630        640        650        660 
EIMAVLALSR SLEDMKQRLA DMVVAFDKRG KPVTADDLGV TGALAVLLKD ALEPNLMQSL 

       670        680        690        700        710        720 
EGTPVLVHAG PFANIAHGCN SIIADEVGLK LVGKNGFVCT EAGFGSDIGM EKFCNIKCRT 

       730        740        750        760        770        780 
SGRKPNAMVL VATVRAIKMH GGGAPVTPGA PLNKQYTEEN LELVQKGLPN LLQHIENGKA 

       790        800        810        820        830        840 
FGMPVVVSLN AHSADTPAEH ELVKKAALEA GAFAAVVSTH WADGGAGAVQ LADAVIKACE 

       850        860        870        880        890        900 
QGNQFRLLYD LELPLVDKMN KIATTMYGAG KVVLSPAAEE KVKRLTDAGF GNLPICMSKV 

       910        920        930        940        950        960 
SGSFTGDAKI KGAPKGFTLD VEDVYVSAGA GFVVAMCGEV TKMPGLPTRP AIYDIDLNTE 


TGEIEGLF 

O96553 in FASTA format

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