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Database: UniProt
Entry: Q4Q9F9_LEIMA
LinkDB: Q4Q9F9_LEIMA
Original site: Q4Q9F9_LEIMA 
ID   Q4Q9F9_LEIMA            Unreviewed;       298 AA.
AC   Q4Q9F9;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 111.
DE   SubName: Full=Putative C-1-tetrahydrofolate synthase,cytoplasmic {ECO:0000313|EMBL:CAJ04615.1};
DE            EC=1.5.1.5 {ECO:0000313|EMBL:CAJ04615.1};
DE            EC=3.5.4.9 {ECO:0000313|EMBL:CAJ04615.1};
GN   ORFNames=LMJF_26_0320 {ECO:0000313|EMBL:CAJ04615.1};
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ04615.1, ECO:0000313|Proteomes:UP000000542};
RN   [1] {ECO:0000313|EMBL:CAJ04615.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=16020728; DOI=10.1126/science.1112680;
RA   Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA   Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA   Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA   Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA   Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA   De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA   Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA   Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA   Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA   Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA   Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA   Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA   Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA   Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA   Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA   Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA   Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA   Barrell B., Myler P.J.;
RT   "The genome of the kinetoplastid parasite, Leishmania major.";
RL   Science 309:436-442(2005).
RN   [2] {ECO:0000313|EMBL:CAJ04615.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
RN   [3] {ECO:0007829|PDB:4A26}
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS).
RX   PubMed=22108435; DOI=10.1016/j.molbiopara.2011.11.004;
RA   Eadsforth T.C., Cameron S., Hunter W.N.;
RT   "The crystal structure of Leishmania major N(5),N(10)-
RT   methylenetetrahydrofolate dehydrogenase/cyclohydrolase and assessment of a
RT   potential drug target.";
RL   Mol. Biochem. Parasitol. 181:178-185(2012).
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777}.
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DR   EMBL; FR796422; CAJ04615.1; -; Genomic_DNA.
DR   RefSeq; XP_001684039.1; XM_001683987.1.
DR   PDB; 4A26; X-ray; 2.70 A; A/B=1-298.
DR   PDBsum; 4A26; -.
DR   AlphaFoldDB; Q4Q9F9; -.
DR   SMR; Q4Q9F9; -.
DR   STRING; 5664.Q4Q9F9; -.
DR   EnsemblProtists; CAJ04615; CAJ04615; LMJF_26_0320.
DR   GeneID; 5652762; -.
DR   KEGG; lma:LMJF_26_0320; -.
DR   VEuPathDB; TriTrypDB:LmjF.26.0320; -.
DR   VEuPathDB; TriTrypDB:LMJFC_260009000; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_260008100; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_260008000; -.
DR   eggNOG; KOG0089; Eukaryota.
DR   HOGENOM; CLU_034045_1_2_1; -.
DR   InParanoid; Q4Q9F9; -.
DR   OMA; VCHILTK; -.
DR   BRENDA; 1.5.1.5; 2950.
DR   BRENDA; 3.5.4.9; 2950.
DR   SABIO-RK; Q4Q9F9; -.
DR   Proteomes; UP000000542; Chromosome 26.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB.
DR   GO; GO:0020023; C:kinetoplast; ISO:GeneDB.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IBA:GO_Central.
DR   GO; GO:0004487; F:methylenetetrahydrofolate dehydrogenase (NAD+) activity; IDA:GeneDB.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR   CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 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   HAMAP; MF_01576; THF_DHG_CYH; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; 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   PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4A26};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAJ04615.1};
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,
KW   ECO:0000313|EMBL:CAJ04615.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000542}.
FT   DOMAIN          7..123
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          127..293
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   298 AA;  31759 MW;  610F5BD725AEF440 CRC64;
     MPSAQIIDGK AIAAAIRSEL KDKVAALREL YGGRVPGLAS IIVGQRMDSK KYVQLKHKAA
     AEVGMASFNV ELPEDISQEV LEVNVEKLNN DPNCHGIIVQ LPLPKHLNEN RAIEKIHPHK
     DADALLPVNV GLLHYKGREP PFTPCTAKGV IVLLKRCGIE MAGKRAVVLG RSNIVGAPVA
     ALLMKENATV TIVHSGTSTE DMIDYLRTAD IVIAAMGQPG YVKGEWIKEG AAVVDVGTTP
     VPDPSRKDGY RLVGDVCFEE AAARAAWISP VPGGVGPMTI AMLLENTLEA FKAALGVS
//
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