ID A0A0P0YDT0_9PROT Unreviewed; 418 AA.
AC A0A0P0YDT0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Aldose 1-epimerase {ECO:0000256|ARBA:ARBA00013185, ECO:0000256|PIRNR:PIRNR005096};
DE EC=5.1.3.3 {ECO:0000256|ARBA:ARBA00013185, ECO:0000256|PIRNR:PIRNR005096};
GN ORFNames=Asbog_00439 {ECO:0000313|EMBL:BAT18748.1};
OS Asaia bogorensis NBRC 16594.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Asaia.
OX NCBI_TaxID=1231624 {ECO:0000313|EMBL:BAT18748.1};
RN [1] {ECO:0000313|EMBL:BAT18748.1, ECO:0000313|Proteomes:UP000068175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16594 {ECO:0000313|EMBL:BAT18748.1,
RC ECO:0000313|Proteomes:UP000068175};
RX PubMed=26358298; DOI=10.1093/dnares/dsv018;
RA Kawai M., Higashiura N., Hayasaki K., Okamoto N., Takami A., Hirakawa H.,
RA Matsushita K., Azuma Y.;
RT "Complete genome and gene expression analyses of Asaia bogorensis reveal
RT unique responses to culture with mammalian cells as a potential
RT opportunistic human pathogen.";
RL DNA Res. 22:357-366(2015).
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|ARBA:ARBA00001614,
CC ECO:0000256|PIRNR:PIRNR005096};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000256|ARBA:ARBA00005028, ECO:0000256|PIRNR:PIRNR005096}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the aldose epimerase family.
CC {ECO:0000256|ARBA:ARBA00006206, ECO:0000256|PIRNR:PIRNR005096}.
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DR EMBL; AP014690; BAT18748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P0YDT0; -.
DR STRING; 1231624.Asbog_00439; -.
DR KEGG; abg:Asbog_00439; -.
DR PATRIC; fig|1231624.3.peg.454; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000068175; Chromosome.
DR GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd09019; galactose_mutarotase_like; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR018052; Ald1_epimerase_CS.
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; ALDOSE-1-EPIMERASE; 1.
DR PANTHER; PTHR10091:SF0; GALACTOSE MUTAROTASE; 1.
DR Pfam; PF01263; Aldose_epim; 1.
DR PIRSF; PIRSF005096; GALM; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR005096};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT BINDING 138..139
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 239..241
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 312
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ SEQUENCE 418 AA; 44717 MW; 8333B97DFD24C2EE CRC64;
MCSPVTNKTP TDKSDTSNRD EAPGTSRTGR TTRPIMALAS GSLAAALSLA SAHAATMSAS
PFGTTQAGQK VEAYTLSAPN GVEVTIMTYG GVILRIMAPD RQGKRDNVVL GYASLAEYEA
KSRANGVFFG ATIGRYANRI AKGRFTLDGH DYAVPVNNGP NSLHGGKDGF DRRIWKAHEI
ARSGNKVGVA LSLISPDGDQ GYPGALNVTV TYTLDDQGAL GIEYKATTSR PTVLNLTNHS
YFNLAGAGSQ DGIFGQMLQI EAHHYTPTDS TLIPTGEIAS VVGTPFDFTT AKPIGRDIRL
ANAQLLMAHG YDHNWVVDDS SSPDGLRHVA TLWDPKSGRS MECLSTEPGV QVYTSNFLDG
SDSGNGHIFR QSDAVTFETQ HFPDSPNQPN FPSTRLNPGQ VFQSRTVFRF GLHESDGK
//
