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Database: UniProt
Entry: G2I712_KOMMN
LinkDB: G2I712_KOMMN
Original site: G2I712_KOMMN 
ID   G2I712_KOMMN            Unreviewed;       398 AA.
AC   G2I712;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|ARBA:ARBA00014165, ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|ARBA:ARBA00013185, ECO:0000256|PIRNR:PIRNR005096};
GN   OrderedLocusNames=GLX_14970 {ECO:0000313|EMBL:BAK83909.1};
OS   Komagataeibacter medellinensis (strain NBRC 3288 / BCRC 11682 / LMG 1693 /
OS   Kondo 51) (Gluconacetobacter medellinensis).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Komagataeibacter.
OX   NCBI_TaxID=634177 {ECO:0000313|EMBL:BAK83909.1, ECO:0000313|Proteomes:UP000009044};
RN   [1] {ECO:0000313|Proteomes:UP000009044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 3288 / BCRC 11682 / LMG 1693
RC   {ECO:0000313|Proteomes:UP000009044};
RX   PubMed=22123756; DOI=10.1128/JB.06158-11;
RA   Ogino H., Azuma Y., Hosoyama A., Nakazawa H., Matsutani M., Hasegawa A.,
RA   Otsuyama K., Matsushita K., Fujita N., Shirai M.;
RT   "Complete genome sequence of NBRC 3288, a unique cellulose-nonproducing
RT   strain of Gluconacetobacter xylinus isolated from vinegar.";
RL   J. Bacteriol. 193:6997-6998(2011).
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   -!- SIMILARITY: Belongs to the aldose epimerase family.
CC       {ECO:0000256|ARBA:ARBA00006206, ECO:0000256|PIRNR:PIRNR005096}.
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DR   EMBL; AP012159; BAK83909.1; -; Genomic_DNA.
DR   RefSeq; WP_014105451.1; NC_016027.1.
DR   AlphaFoldDB; G2I712; -.
DR   STRING; 634177.GLX_14970; -.
DR   KEGG; gxy:GLX_14970; -.
DR   PATRIC; fig|634177.7.peg.1714; -.
DR   eggNOG; COG2017; Bacteria.
DR   HOGENOM; CLU_031753_2_0_5; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000009044; 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:SF50; 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.
DR   PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR005096};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..398
FT                   /note="Aldose 1-epimerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003431422"
FT   ACT_SITE        218
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        356
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         117..118
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         218..220
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         290
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   398 AA;  42816 MW;  48E5D0292A39C593 CRC64;
     MRATLPCKSH LLLLATWLLA ALPATVAWAT PQPVTITRAP FGTLADGQTV EQFTLANGRG
     MSVRVMTYGA IITAIDVPDR WGHVADVVLG FPTLEGYVVN NPRGSLYFGA TVGRVANRIR
     GGSFTLDGRT YHIPQTEGTN ALHGGRQGFD RHVWSVETIT TTPQAASVTL MRVSPDGEEG
     FPGTLTTHVT FGLNTRNELS LHYRATTDRP TVVNLTNHSY FNLGGEGSGS VESEILQIHA
     DTFTPVDAQS LPLGTIAPVA GTALDFRMPR RIGAGLRDGG QQMLFQRGYD HNWIVGGTPT
     RAPIPAAHLS DPASGRNMDV LTTQPGLQVY TANALDGRYS GPAGHAYRQT DAVALEAEHY
     PDSPNHPDFP TITLRPGETY DQTTIYRLGV EPMGHGTP
//
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