ID I1KZJ0_SOYBN Unreviewed; 439 AA.
AC I1KZJ0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KRH46895.1, ECO:0000313|EnsemblPlants:KRH46895};
GN Name=100807267 {ECO:0000313|EnsemblPlants:KRH46895};
GN ORFNames=GLYMA_08G362900 {ECO:0000313|EMBL:KRH46895.1};
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:KRH46895};
RN [1] {ECO:0000313|EMBL:KRH46895.1, ECO:0000313|EnsemblPlants:KRH46895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH46895};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH46895.1};
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:KRH46895}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH46895};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH46895.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH46895.1};
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; CM000841; KRH46895.1; -; Genomic_DNA.
DR RefSeq; XP_003532330.1; XM_003532282.2.
DR AlphaFoldDB; I1KZJ0; -.
DR SMR; I1KZJ0; -.
DR STRING; 3847.I1KZJ0; -.
DR PaxDb; 3847-GLYMA08G47790-1; -.
DR EnsemblPlants; KRH46895; KRH46895; GLYMA_08G362900.
DR GeneID; 100807267; -.
DR Gramene; KRH46895; KRH46895; GLYMA_08G362900.
DR KEGG; gmx:100807267; -.
DR eggNOG; KOG2772; Eukaryota.
DR InParanoid; I1KZJ0; -.
DR OrthoDB; 1207763at2759; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000008827; Chromosome 8.
DR ExpressionAtlas; I1KZJ0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; 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 PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827}.
SQ SEQUENCE 439 AA; 47944 MW; 21E1BE835C904BE7 CRC64;
MASIFKLSTP SPAASLSEAL RPRDSRFLSF NPSSNAINYK INLSASLRSI HSLPLKTSLR
IKCSQTDGNG SPAKRTVLHD LYEKEGQSPW YDNLCRPVTD LLPLIASGVR GVTSNPAIFQ
KAISSSNAYN DQFRELVQAG KDIESAYWEL VVKDIQDACK LFEPIYDQTD GGDGYVSVEV
SPRLADDTEG TIEAAKWLHK VVDRPNVYIK IPATEACVPS IKEVIANGIS VNVTLIFSLA
RYEAVIDAYL DGLEASGLND LSRVTSVASF FVSRVDTLID KALEKIGTPE ALNLRGKAAV
AQAALAYQLY QRKFSGPRWE ALVKKGAKKQ RLLWASTSVK NPAYSDTLYV APLIGPDTVS
TMPDQALQAF IDHGTVSRTI DSNASEAEGI YNALQKLGID WSFVGSQLEL EGVDSFKKSF
DSLLDSLQEK ANSLKLVSH
//
