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Database: UniProt
Entry: K7MVK2_SOYBN
LinkDB: K7MVK2_SOYBN
Original site: K7MVK2_SOYBN 
ID   K7MVK2_SOYBN            Unreviewed;       396 AA.
AC   K7MVK2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KRH01793.1, ECO:0000313|EnsemblPlants:KRH01793};
GN   Name=100816075 {ECO:0000313|EnsemblPlants:KRH01793};
GN   ORFNames=GLYMA_18G299100 {ECO:0000313|EMBL:KRH01793.1};
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|EnsemblPlants:KRH01793};
RN   [1] {ECO:0000313|EMBL:KRH01793.1, ECO:0000313|EnsemblPlants:KRH01793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH01793};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH01793.1};
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:KRH01793}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH01793};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH01793.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH01793.1};
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: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000256|ARBA:ARBA00003518}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         beta-D-fructose 6-phosphate + D-erythrose 4-phosphate;
CC         Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001469};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC       {ECO:0000256|ARBA:ARBA00004959}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008426}.
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DR   EMBL; CM000851; KRH01793.1; -; Genomic_DNA.
DR   AlphaFoldDB; K7MVK2; -.
DR   EnsemblPlants; KRH01793; KRH01793; GLYMA_18G299100.
DR   Gramene; KRH01793; KRH01793; GLYMA_18G299100.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000008827; Chromosome 18.
DR   ExpressionAtlas; K7MVK2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   CDD; cd00955; Transaldolase_like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00493; Transaldolase_2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004732; Transaldolase_2.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   NCBIfam; TIGR00876; tal_mycobact; 1.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   PANTHER; PTHR10683:SF31; TRANSALDOLASE; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        366..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   396 AA;  43761 MW;  2DA36EBD57AC8D6D CRC64;
     MASVSKLSTP NPLASLSEAL RPRDSRFLTF KPSSIAFNHK TNLSASLRSI HSLPLKTSLR
     IKCSQTDGNG SPAKRTVLHD LYEKEGQSPW YDNLCRPVTD LLPLIASGVR GVTSNPAIFQ
     KAISSSNAYN DQFRELVQTG KDIESAYWEL VVKDIQDACR LFEPIYDQTD GGDGYVSVEV
     SPRLADDTEG TIEAAKWLHK VVDRPNVYIK IPATEACVPS IKEVIANGIS VNVTLIFSLA
     RYEAVIDAYL DGLEASELND LSRVTSVASF FVSRVDTLID KALEKIGTPV ALNLRGKAAV
     AQAALAYQLY QRKFSGPRWE ALVKKGAKKQ RLLWASTSVK NPAYSDTLYV APLIGPDTVS
     HHFFHFLNLF IIMIGLILKL ILLALMDLFV VWPCLF
//
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