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Database: UniProt
Entry: A0A495SH83_9FLAO
LinkDB: A0A495SH83_9FLAO
Original site: A0A495SH83_9FLAO 
ID   A0A495SH83_9FLAO        Unreviewed;       393 AA.
AC   A0A495SH83;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN   ORFNames=C8C88_1381 {ECO:0000313|EMBL:RKS99590.1};
OS   Flavobacterium sp. 123.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2135627 {ECO:0000313|EMBL:RKS99590.1, ECO:0000313|Proteomes:UP000271452};
RN   [1] {ECO:0000313|EMBL:RKS99590.1, ECO:0000313|Proteomes:UP000271452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=123 {ECO:0000313|EMBL:RKS99590.1,
RC   ECO:0000313|Proteomes:UP000271452};
RA   Chistoserdova L.;
RT   "Synthetic bacterial communities of pure cultures isolated from sediment of
RT   Lake Washington, USA.";
RL   Submitted (OCT-2018) 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:RKS99590.1}.
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DR   EMBL; RBXD01000001; RKS99590.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495SH83; -.
DR   OrthoDB; 9779408at2; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000271452; 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:UP000271452}.
FT   ACT_SITE        221
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        358
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         121..122
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         221..223
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         293
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   393 AA;  43333 MW;  A9EF9A364B1E8B60 CRC64;
     MNVLKRCIYG ISILSLASMN VQCKSDKKSE ETSKEATTAE VVTIAKSAYG TTEKGEKVDS
     YKLTNQKGME VNIITYGGII SSLKVPNKAG KSEEVVIGFN SLDQYMKANP YFGALIGRYG
     NRIAKGKFTL DGKEYSLAIN NEPNALHGGP EGFHRVVWTA EEAKGGDSAS LKLKYVSKDM
     EEGYPGNLTV FVTYTLHNDN SLDVLYEATT DKKTVVNLTQ HSYFNLSSDF SKPILDHEIT
     IDADKLVPVA ATLIPTGKLT DVTNTPFDFR KPKAIGAAIE AKDEQLKNGL GYDHCWVLNN
     QGKGERFAAS AYEATSGRLL EVYTDQPGIQ FYSGNFLDGT LPMRNGGTYA RRTGFCLETQ
     HYPDSPNQKD FPTTVLNPDE NYKTKTTFKF SVK
//
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