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Database: UniProt
Entry: B9R7Y4_RICCO
LinkDB: B9R7Y4_RICCO
Original site: B9R7Y4_RICCO 
ID   B9R7Y4_RICCO            Unreviewed;       591 AA.
AC   B9R7Y4;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Bifunctional dihydrofolate reductase-thymidylate synthase {ECO:0000256|PIRNR:PIRNR000389};
GN   ORFNames=RCOM_1595270 {ECO:0000313|EMBL:EEF52614.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
CC   -!- FUNCTION: Bifunctional enzyme. Involved in de novo dTMP biosynthesis.
CC       Key enzyme in folate metabolism. Can play two different roles depending
CC       on the source of dihydrofolate: de novo synthesis of tetrahydrofolate
CC       or recycling of the dihydrofolate released as one of the end products
CC       of the TS catalyzed reaction. 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:ARBA00024992}.
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC       tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004903, ECO:0000256|PIRNR:PIRNR000389}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the thymidylate
CC       synthase family. {ECO:0000256|PIRNR:PIRNR000389}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the dihydrofolate
CC       reductase family. {ECO:0000256|PIRNR:PIRNR000389}.
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DR   EMBL; EQ973772; EEF52614.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9R7Y4; -.
DR   STRING; 3988.B9R7Y4; -.
DR   eggNOG; KOG0673; Eukaryota.
DR   eggNOG; KOG1324; Eukaryota.
DR   InParanoid; B9R7Y4; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IBA:GO_Central.
DR   GO; GO:0004799; F:thymidylate synthase activity; IBA:GO_Central.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00209; DHFR; 1.
DR   CDD; cd00351; TS_Pyrimidine_HMase; 1.
DR   Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR   Gene3D; 3.30.572.10; Thymidylate synthase/dCMP hydroxymethylase domain; 1.
DR   HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR   InterPro; IPR024072; DHFR-like_dom_sf.
DR   InterPro; IPR012262; DHFR-TS.
DR   InterPro; IPR017925; DHFR_CS.
DR   InterPro; IPR001796; DHFR_dom.
DR   InterPro; IPR045097; Thymidate_synth/dCMP_Mease.
DR   InterPro; IPR023451; Thymidate_synth/dCMP_Mease_dom.
DR   InterPro; IPR036926; Thymidate_synth/dCMP_Mease_sf.
DR   InterPro; IPR000398; Thymidylate_synthase.
DR   NCBIfam; TIGR03284; thym_sym; 1.
DR   PANTHER; PTHR11548:SF2; THYMIDYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11548; THYMIDYLATE SYNTHASE 1; 1.
DR   Pfam; PF00186; DHFR_1; 1.
DR   Pfam; PF00303; Thymidylat_synt; 1.
DR   PIRSF; PIRSF000389; DHFR-TS; 1.
DR   PRINTS; PR00108; THYMDSNTHASE.
DR   SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR   SUPFAM; SSF55831; Thymidylate synthase/dCMP hydroxymethylase; 1.
DR   PROSITE; PS00075; DHFR_1; 1.
DR   PROSITE; PS51330; DHFR_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR000389}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide biosynthesis {ECO:0000256|PIRNR:PIRNR000389};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW   ECO:0000256|PIRNR:PIRNR000389};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000389};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000389}.
FT   DOMAIN          86..263
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
FT   ACT_SITE        470
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000389-1"
SQ   SEQUENCE   591 AA;  66644 MW;  3BDCC6A10AEF4B2B CRC64;
     MYGKIRLAFR RYLDFDAAML TRVLLSSCKN SFWNSSYLSV AVTRLQIVSC ESPKWRSYRR
     LSVMSGDVSI GIPRGNANMH LDRNRRYQVV VAATRDMGIG KDGKLPWRLP SDLKFFKELT
     LTTSSPGKRN AVVMGRKTWE SIPLKYRPLP GRLNIVLTCS GGCDITTAED VLTCGSIPSA
     LELLAEAPYS FLIEKVFFIG GGQILRKTIN APGCDAIHIT EIETSIECDT FIPVIDFSLF
     HPWYSSLPIV ENNVRYSFAT YVRVKNSENG TLSKSASANG NLSSNTFEVK NFTFLPSIIY
     KKHDEYMYLR LAEQIISNGT LKDDRTGTGT LSKFGGQMQY NLRKSFPLLT TKRVFWMGVV
     EELLWFISGS TNAKVLQEKG IHIWDGNASR DYLDSIGLKD IEESDLGPIY GFQWRYFGAR
     YTDMHADYSG QGFDQLVDVI DKIKSKPDDR CIILRSWNPS DLKLMAFPPC HMFAQFYVAN
     GELSCQMYQR SADIGLGVPF NIAFYALLTC IIAHVCALVP GDFIHLIGDA RVCTTHIGPL
     QKQLQKLPTP FPILRINPAK KDIDSFEASD FQLIGYDPHE YIDMKNLSVD L
//
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