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Database: UniProt
Entry: A0A150ALE9_9BACT
LinkDB: A0A150ALE9_9BACT
Original site: A0A150ALE9_9BACT 
ID   A0A150ALE9_9BACT        Unreviewed;       353 AA.
AC   A0A150ALE9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN   ORFNames=AVL50_07860 {ECO:0000313|EMBL:KXX70720.1};
OS   Flammeovirga sp. SJP92.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Flammeovirga.
OX   NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX70720.1, ECO:0000313|Proteomes:UP000075267};
RN   [1] {ECO:0000313|EMBL:KXX70720.1, ECO:0000313|Proteomes:UP000075267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJP92 {ECO:0000313|EMBL:KXX70720.1,
RC   ECO:0000313|Proteomes:UP000075267};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXX70720.1}.
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DR   EMBL; LQAQ01000042; KXX70720.1; -; Genomic_DNA.
DR   RefSeq; WP_062616520.1; NZ_LQAQ01000042.1.
DR   AlphaFoldDB; A0A150ALE9; -.
DR   STRING; 1775430.AVL50_07860; -.
DR   OrthoDB; 9779408at2; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000075267; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR005096};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075267}.
FT   ACT_SITE        184
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        318
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         83..84
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         184..186
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         254
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   353 AA;  39127 MW;  C3067BBC394D5D9E CRC64;
     MIDIKQIEKV AWGKHDDKDV YLYTLTNQKG SQLKVSTYGG ILVSFVTADK NGEMADVLLG
     KDSLEDYLKN DCYLGATVGQ FANRIAKGKI SIDGVEYQLA TNNGPNFLHG GDKGFDSHVF
     DIVEEISEEN VSSVVLSHTS PDGFENLPGN VTLKLKISLT DENEIVLDYS ATTDKKTIVN
     FTSHPYFNLK GEGEITDHSL LLNCKYYTPV DETCIPTGEI VSVKGTPFDF TEEKVIGNEI
     DADHDQTQIG IGYDHNLVIN KPVGEYGLVG IAYEATTGRS MEVYSTEPGV QFYTGNWLEG
     DLGKNQTAHI KRQGFCLEAQ HFPDSPNQPH FPSVILNPNE EYTQKTVYKF VVK
//
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