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Database: UniProt
Entry: A0A212TNM5_9BACT
LinkDB: A0A212TNM5_9BACT
Original site: A0A212TNM5_9BACT 
ID   A0A212TNM5_9BACT        Unreviewed;       359 AA.
AC   A0A212TNM5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=SAMN06265337_2008 {ECO:0000313|EMBL:SNC67602.1};
OS   Hymenobacter gelipurpurascens.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=89968 {ECO:0000313|EMBL:SNC67602.1, ECO:0000313|Proteomes:UP000198131};
RN   [1] {ECO:0000313|EMBL:SNC67602.1, ECO:0000313|Proteomes:UP000198131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11116 {ECO:0000313|EMBL:SNC67602.1,
RC   ECO:0000313|Proteomes:UP000198131};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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|ARBA:ARBA00001614,
CC         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   -!- 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; FYEW01000001; SNC67602.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212TNM5; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000198131; 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; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
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   ACT_SITE        195
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        323
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         95..96
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         195..197
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         259
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   359 AA;  38131 MW;  38DBFD017DE0B150 CRC64;
     MASSSTSTQG AAPTSASFGK TTDGTEVQLF TLTNAHGLKV SITNYGGTVT SLLVPDKAGK
     LGDVVLGFDN VSGYQSPAFL KSGPYFGALI GRYGNRIAKG KFTLDGKQYT LANNNGENTL
     HGGKKGFDKV VWQATPGTSA EGQTLTLTYL SQDGEEGYPG NLQVTVVYTL TPDDALKIDY
     SATTDKATPV NLTNHAYFNL SGGNDVLGHQ VTLPADRYTV VDAGLIPTGE LRPVKGTPFD
     FTSPHAIGER IGQVPGGYDH NWVLNEAKGM HAAATVYEPT TGRTMEVRTT EPGIQFYTGN
     FLDGTLKGKG GQVYGKHAGF CLETQHFPDS PNQPSFPSTI LKPGQTLHST TTYTFGVRQ
//
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