ID I1IYF8_BRADI Unreviewed; 363 AA.
AC I1IYF8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN Name=100843923 {ECO:0000313|EnsemblPlants:KQJ82952};
GN ORFNames=BRADI_5g12250v3 {ECO:0000313|EMBL:KQJ82952.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:KQJ82952};
RN [1] {ECO:0000313|EMBL:KQJ82952.1, ECO:0000313|EnsemblPlants:KQJ82952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ82952.1,
RC ECO:0000313|EnsemblPlants:KQJ82952};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ82952.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ82952.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ82952}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ82952};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose = beta-D-glucose; Xref=Rhea:RHEA:10264,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:17925; EC=5.1.3.3;
CC Evidence={ECO:0000256|PIRNR:PIRNR005096};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000256|ARBA:ARBA00005028, ECO:0000256|PIRNR:PIRNR005096}.
CC -!- SIMILARITY: Belongs to the aldose epimerase family.
CC {ECO:0000256|ARBA:ARBA00006206, ECO:0000256|PIRNR:PIRNR005096}.
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DR EMBL; CM000884; KQJ82952.1; -; Genomic_DNA.
DR RefSeq; XP_003579891.1; XM_003579843.3.
DR AlphaFoldDB; I1IYF8; -.
DR STRING; 15368.I1IYF8; -.
DR EnsemblPlants; KQJ82952; KQJ82952; BRADI_5g12250v3.
DR GeneID; 100843923; -.
DR Gramene; KQJ82952; KQJ82952; BRADI_5g12250v3.
DR KEGG; bdi:100843923; -.
DR eggNOG; KOG1604; Eukaryota.
DR HOGENOM; CLU_031753_4_2_1; -.
DR InParanoid; I1IYF8; -.
DR OMA; SIRMHAT; -.
DR OrthoDB; 334899at2759; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000008810; Chromosome 5.
DR GO; GO:0004034; F:aldose 1-epimerase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR CDD; cd09019; galactose_mutarotase_like; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR015443; Aldose_1-epimerase.
DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR047215; Galactose_mutarotase-like.
DR InterPro; IPR014718; GH-type_carb-bd.
DR PANTHER; PTHR10091:SF28; ALDOSE 1-EPIMERASE; 1.
DR PANTHER; PTHR10091; ALDOSE-1-EPIMERASE; 1.
DR Pfam; PF01263; Aldose_epim; 1.
DR PIRSF; PIRSF005096; GALM; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR005096};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..363
FT /note="Aldose 1-epimerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014095611"
FT ACT_SITE 194
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT ACT_SITE 328
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT BINDING 92..93
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 194..196
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 263
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ SEQUENCE 363 AA; 39239 MW; 947E1872316D652F CRC64;
MAGAAVLPIA FLLCLALAGG ADAAGKAVGF YELKNKKGDF SIKVTNWGAA LVSVVVPDCK
GNLDDVVLGY DTVAAYVNGS GSFGATVGRV ANRIANSRFV LDGKAYRLFR NDGNNSIHGG
HRGFGKVIWT VKEYVRDGDS PYITFFYHSF DGEQGFPGDL DVYVTYQLSS PYVLSIRMHA
TALSKATPVN LANHAYWNLG GHGSGDVLKH ELQLLASRYT PLDKSKIPTG QIAAVSGTMY
DFLAPKPVGK HMEIVPGGGG GYDINYAVDG EDQYAMRRVA RVRDPASGRA MEVWANQPGV
QLYTSNWVIN EKGKAGKVYQ QYGALCLETQ AYPDAVNHPE FPSSIVRPGQ AYKHDMEIKF
SAH
//
