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Database: UniProt
Entry: A0A0E0R8F8_ORYRU
LinkDB: A0A0E0R8F8_ORYRU
Original site: A0A0E0R8F8_ORYRU 
ID   A0A0E0R8F8_ORYRU        Unreviewed;       521 AA.
AC   A0A0E0R8F8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Bifunctional dihydrofolate reductase-thymidylate synthase {ECO:0000256|PIRNR:PIRNR000389};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI11G14530.1, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA   Zhao Q.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORUFI11G14530.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-
CC         dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422;
CC         EC=2.1.1.45; Evidence={ECO:0000256|ARBA:ARBA00001707};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate +
CC         H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.5.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001315};
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|ARBA:ARBA00006900,
CC       ECO:0000256|PIRNR:PIRNR000389}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the dihydrofolate
CC       reductase family. {ECO:0000256|ARBA:ARBA00010176,
CC       ECO:0000256|PIRNR:PIRNR000389}.
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DR   AlphaFoldDB; A0A0E0R8F8; -.
DR   STRING; 4529.A0A0E0R8F8; -.
DR   EnsemblPlants; ORUFI11G14530.1; ORUFI11G14530.1; ORUFI11G14530.
DR   Gramene; ORUFI11G14530.1; ORUFI11G14530.1; ORUFI11G14530.
DR   eggNOG; KOG0673; Eukaryota.
DR   eggNOG; KOG1324; Eukaryota.
DR   HOGENOM; CLU_021669_2_2_1; -.
DR   OMA; SIPWRVP; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000008022; Unassembled WGS sequence.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:InterPro.
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   InterPro; IPR020940; Thymidylate_synthase_AS.
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.
DR   PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR000389};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727,
KW   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:UP000008022};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000389}.
FT   DOMAIN          17..194
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
FT   ACT_SITE        403
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000389-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10016"
SQ   SEQUENCE   521 AA;  58592 MW;  72E26D4009D97614 CRC64;
     MATTLSNGVS QNGPQRNYQV VVAATRDMGI GKDGVLPWKL LGDLKFFKEL TVTTADPVKK
     NAVIMGRKTW ESLPLKARPL PGRLNIILTR SGSFEFATVE NVVICGSMNS ALELLSSTPY
     CLSIEKVFVI GGGQVLRESL NGPSCEAVHL TDIQSSIECD TFIPPIDLSV FQPWYSSLPV
     VESNIRHSFV TYVRVRKTMA ETHDSNGKES ANDGIKSDKF ETENFSFLPK LIFDRHEEYH
     YLNLVEDIIR SGAQKNDRTG TGTLSKFGCQ MRFNLRNSFP LLTTKKVFWR GVVEELLWFI
     SGLTSAKVLQ EKGIHIWDGN ASREYLDSVG LAHREEGDLG PVYGFQWRHF GAEYTDMHAD
     YTGKGFDQLM DVIDKIKNNP DDRRIILSAW NPSDLKKMAL PPCHMFAQFY VESGELSCQM
     YQRSADMGLG VPFNIASYSL LTYMIAHVCG LSPGEFVHVI GDAHVYRTHV RALEEQIQKL
     PKPFPILKIN PLKKDIDSFV ASDFKLVGYD PHQKIEMKMA I
//
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