ID A0A182LWE5_9DIPT Unreviewed; 1050 AA.
AC A0A182LWE5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=C-1-tetrahydrofolate synthase, cytoplasmic {ECO:0000256|ARBA:ARBA00017592};
DE EC=1.5.1.5 {ECO:0000256|ARBA:ARBA00012859};
DE EC=3.5.4.9 {ECO:0000256|ARBA:ARBA00012776};
DE EC=6.3.4.3 {ECO:0000256|ARBA:ARBA00012295};
OS Anopheles culicifacies.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; culicifacies species complex.
OX NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA003570-PA, ECO:0000313|Proteomes:UP000075883};
RN [1] {ECO:0000313|Proteomes:UP000075883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles culicifacies species A.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACUA003570-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA003570-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-
CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455,
CC ChEBI:CHEBI:195366; EC=3.5.4.9;
CC Evidence={ECO:0000256|ARBA:ARBA00036357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-10-
CC formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:195366, ChEBI:CHEBI:456216;
CC EC=6.3.4.3; Evidence={ECO:0000256|ARBA:ARBA00036012};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000256|ARBA:ARBA00004777}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC formate--tetrahydrofolate ligase family.
CC {ECO:0000256|ARBA:ARBA00006985}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000256|ARBA:ARBA00005559}.
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DR EMBL; AXCM01002203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182LWE5; -.
DR STRING; 139723.A0A182LWE5; -.
DR EnsemblMetazoa; ACUA003570-RA; ACUA003570-PA; ACUA003570.
DR VEuPathDB; VectorBase:ACUA003570; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000075883; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00477; FTHFS; 1.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01543; FTHFS; 1.
DR HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR000559; Formate_THF_ligase.
DR InterPro; IPR020628; Formate_THF_ligase_CS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000672; THF_DH/CycHdrlase.
DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR InterPro; IPR020867; THF_DH/CycHdrlase_CS.
DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR PANTHER; PTHR48099:SF5; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 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 SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00721; FTHFS_1; 1.
DR PROSITE; PS00766; THF_DHG_CYH_1; 1.
DR PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 121..239
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 243..406
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 1050 AA; 112895 MW; 8C6013D5328CE908 CRC64;
MIANDTADRE RSSCAPLPKL VRDCDASPAP SVPSGRSLET HVTFCGPPSN PSSDQRYSSA
LSTIGTLVDI GTAALETSRK FVSELVALRP PDVAETRKKA PGERYSSSNK CDTMLSGAKI
LSGTDVAKEI RERLKKEVAE IRRQIPTLVP GLAIVQVGGR EDSNVYIRMK IKAAEEIGMY
AEHVQLPRST TQDELLATVK RLNEDPCFHG IIVQMPLDSE TPIDAHLVTD AVSPEKDVDG
LNTINEGRVA TGDMSGFLPC TPNGCMELIK RTGTPIAGSY AVVIGRSKIV GTPMSELLKW
ADATVTVAHS KTKNLNLLIK KADILVVAVG RPEMVRGAWI KPGAVVIDCG INSIPDPTKK
SGQRLVGDVK YEEALPVASH VTPVPGGVGP MTVAMLMQNT VQSAQRVARR LIEMEFRWCL
KPLPLKLTEP VPSDIEIARA QEPKDVSVLA QEIGLIPSEV SLYGTKKAKV SLKVLERLQY
EDDAKYVVVA GITPTPLGEG KSTTLVGLVQ ALTAYKRCNS IACLRQPSQG PTFGIKGGAA
GGGYSQVIPM EDFNLHLTGD IHAVTAANNL LAAQLDARIF HEATQTDQAL YERLVPAVKG
SRKFAPIQLR RLKRLGIEKT DPYALTPDEI RRFARLNIDP HNVVWTRVLD VNDRYLRKIT
IGLSPTEKNL TRDTSFAISV SSEIMAILAL ATGLEDMKQR LAKMVVAFDK TGAPVTADDL
GVTGSMMVLL KDAIEPTLMQ TLEGTPVLVH AGPFANIAHG CSSIVADDIG MKLAGKRGYV
VTEAGFGSDI GMEKFFNIKC RASGKVPNAV VLVTTVRALK MHGGGPIVTA GAPLRREYMS
ENLDLLEKGL PNLLKHIENG LKFGVPVVVA INAHGTDTPA EHELVRKAAK AAGAFDAIVS
NHWAKGGEGA ADLAQAVIEA CNRPSEFKLL YEVDMPIEDK IICIAKEMYG AGTIELNSKV
RDAIRLYTEK GFGKLPICMA KTSMSLTGDP SVKGAPKDFK LVINDICLSA GAGFIVPMCG
EISKMPGLPT RPSIFDIDLN TETGEIEGLF
//
