GenomeNet

Database: UniProt
Entry: I1LQ11_SOYBN
LinkDB: I1LQ11_SOYBN
Original site: I1LQ11_SOYBN 
ID   I1LQ11_SOYBN            Unreviewed;       530 AA.
AC   I1LQ11;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Bifunctional dihydrofolate reductase-thymidylate synthase {ECO:0000256|PIRNR:PIRNR000389};
GN   Name=100788658 {ECO:0000313|EnsemblPlants:KRH24440};
GN   ORFNames=GLYMA_12G041000 {ECO:0000313|EMBL:KRH24441.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH24441.1};
RN   [1] {ECO:0000313|EMBL:KRH24441.1, ECO:0000313|EnsemblPlants:KRH24440}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH24440};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH24441.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH24440}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH24440};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH24441.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH24441.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM000845; KRH24440.1; -; Genomic_DNA.
DR   EMBL; CM000845; KRH24441.1; -; Genomic_DNA.
DR   RefSeq; XP_003541010.1; XM_003540962.3.
DR   AlphaFoldDB; I1LQ11; -.
DR   SMR; I1LQ11; -.
DR   STRING; 3847.I1LQ11; -.
DR   PaxDb; 3847-GLYMA12G04480-2; -.
DR   EnsemblPlants; KRH24440; KRH24440; GLYMA_12G041000.
DR   EnsemblPlants; KRH24441; KRH24441; GLYMA_12G041000.
DR   GeneID; 100788658; -.
DR   Gramene; KRH24440; KRH24440; GLYMA_12G041000.
DR   Gramene; KRH24441; KRH24441; GLYMA_12G041000.
DR   KEGG; gmx:100788658; -.
DR   HOGENOM; CLU_021669_2_2_1; -.
DR   InParanoid; I1LQ11; -.
DR   OMA; ILCAWNV; -.
DR   OrthoDB; 1118873at2759; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000008827; Chromosome 12.
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; 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; 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   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|PIRNR:PIRNR000389};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000389}.
FT   DOMAIN          26..203
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        412
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000389-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10016"
SQ   SEQUENCE   530 AA;  59902 MW;  BD1869A3537334DF CRC64;
     MATDALVISN GNGNGNAKSE LHPQRTYQVV VVATRDMGIS KDAKLPWTLP TELKFFEEIT
     TTTSDPGKKN AVVMGRKTWE SIPPENRPLP GRLNVVLTRS GSFDIATAEN VLICGSMASA
     MELLASSPYC LSIEKVFLTG GGEIFREALN APGCEAAHIT EIEASIECDT FMPRVDTNVF
     QTWYSSFPLV EDNLRYSFTT YARVRSSPPE FLDQNADPFF YNNSDSFKFE VKKFSFLPKM
     VYERHEEFKY LRLVQEIISE GTTKDDRTGT GTLSKFGCQM RFNLRRNFPL LTTKKVFWRG
     VVEELLWFIS GSTSAKALQE KGIHIWDGNA SREYLDSIGL TEREKGDLGP VYGFQWRHFG
     AKYTDMHADY SGQGFDQLLD VINKIKHNPN DRRIILSAWN PSDLKLMALP PCHMFAQFYV
     ANGELSCQMY QRSADMGLGV PFNIASYALL TCMIAHVCDL VPGDFIHVIG DAHVYRNHVR
     PLQEQLQNQP KPFPILKINP KKKDIDSFVA ADFKLIGYDP HQKIEMKMAV
//
DBGET integrated database retrieval system