ID B8BYC4_THAPS Unreviewed; 214 AA.
AC B8BYC4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Bifunctional dihydrofolate reductase-thymidylate synthase {ECO:0000256|ARBA:ARBA00019798};
DE EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
DE EC=2.1.1.45 {ECO:0000256|ARBA:ARBA00011947};
GN ORFNames=THAPSDRAFT_261857 {ECO:0000313|EMBL:EED94350.1};
OS Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=35128 {ECO:0000313|EMBL:EED94350.1, ECO:0000313|Proteomes:UP000001449};
RN [1] {ECO:0000313|EMBL:EED94350.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED94350.1};
RX PubMed=15459382; DOI=10.1126/science.1101156;
RA Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA Wilkerson F.P., Rokhsar D.S.;
RT "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT metabolism.";
RL Science 306:79-86(2004).
RN [2] {ECO:0000313|EMBL:EED94350.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED94350.1};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
CC -!- FUNCTION: Bifunctional enzyme. Involved in de novo dTMP biosynthesis.
CC Key enzyme in folate metabolism. Catalyzes an essential reaction for de
CC novo glycine and purine synthesis, DNA precursor synthesis, and for the
CC conversion of dUMP to dTMP. {ECO:0000256|ARBA:ARBA00025154}.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004903}.
CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC {ECO:0000256|RuleBase:RU004474}.
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DR EMBL; CM000640; EED94350.1; -; Genomic_DNA.
DR RefSeq; XP_002288914.1; XM_002288878.1.
DR AlphaFoldDB; B8BYC4; -.
DR STRING; 35128.B8BYC4; -.
DR PaxDb; 35128-Thaps261857; -.
DR EnsemblProtists; EED94350; EED94350; THAPSDRAFT_261857.
DR GeneID; 7451283; -.
DR KEGG; tps:THAPSDRAFT_261857; -.
DR HOGENOM; CLU_043966_5_1_1; -.
DR InParanoid; B8BYC4; -.
DR OMA; NISCWIA; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000001449; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046452; P:dihydrofolate metabolic process; IBA:GO_Central.
DR GO; GO:0046655; P:folic acid metabolic process; IBA:GO_Central.
DR GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IBA:GO_Central.
DR CDD; cd00209; DHFR; 1.
DR Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR InterPro; IPR012259; DHFR.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR017925; DHFR_CS.
DR InterPro; IPR001796; DHFR_dom.
DR PANTHER; PTHR48069; DIHYDROFOLATE REDUCTASE; 1.
DR PANTHER; PTHR48069:SF3; DIHYDROFOLATE REDUCTASE; 1.
DR Pfam; PF00186; DHFR_1; 1.
DR PRINTS; PR00070; DHFR.
DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR PROSITE; PS00075; DHFR_1; 1.
DR PROSITE; PS51330; DHFR_2; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001449}.
FT DOMAIN 18..214
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
SQ SEQUENCE 214 AA; 23877 MW; A249C109A0470056 CRC64;
MQSQQFTSNA LAKQYTQSFG IVAALTKNGV IGINGSLPWE SLTQDRDHFI NLTRGKVLIL
GRKTFVDEDP SGGHVDHARA CIVVSSTMYY SRSHGSTLVK VARSLDEALV MANKLNTSSG
ITKTRNSSID CWVAGGERLY KDALQHPCAA EVHLTQVDIT ISTDMLATKD EVAYFPVDYL
NNYGFQEVSK REDGICVFCV YKRQTQRVRE IECW
//
