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Database: UniProt
Entry: A0A0A6Y458_9BACT
LinkDB: A0A0A6Y458_9BACT
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ID   A0A0A6Y458_9BACT        Unreviewed;       376 AA.
AC   A0A0A6Y458;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|ARBA:ARBA00014165};
DE            EC=5.1.3.3 {ECO:0000256|ARBA:ARBA00013185};
DE   AltName: Full=Galactose mutarotase {ECO:0000256|ARBA:ARBA00033373};
DE   AltName: Full=Type-1 mutarotase {ECO:0000256|ARBA:ARBA00032300};
DE   Flags: Fragment;
GN   ORFNames=AH06_01320 {ECO:0000313|EMBL:KHD90154.1};
OS   candidate division TM6 bacterium Zodletone_IIa.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=1511133 {ECO:0000313|EMBL:KHD90154.1, ECO:0000313|Proteomes:UP000242648};
RN   [1] {ECO:0000313|EMBL:KHD90154.1, ECO:0000313|Proteomes:UP000242648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zodletone_IIa {ECO:0000313|EMBL:KHD90154.1};
RA   Doloman A., Krumholz L.R.;
RT   "Metabolic reconstruction of the genome of Candidate Division TM6,
RT   uncultured bacterial phylum in Zodletone spring, Oklahoma.";
RL   Submitted (JUN-2014) 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   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000256|ARBA:ARBA00005028}.
CC   -!- SIMILARITY: Belongs to the aldose epimerase family.
CC       {ECO:0000256|ARBA:ARBA00006206}.
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:KHD90154.1}.
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DR   EMBL; JOKC01000145; KHD90154.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A6Y458; -.
DR   PATRIC; fig|1511133.3.peg.151; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000242648; 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: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   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242648}.
FT   ACT_SITE        202
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        340
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         103..104
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         202..204
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         274
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KHD90154.1"
SQ   SEQUENCE   376 AA;  40667 MW;  6C87BE8BCDAFE620 CRC64;
     CGNSNNGTAT EKPADSTVAT APALPDAKNF TDSVDGKATS LYILKNKNNA TAAITSYGAR
     VVSLLVPDKN GVMTDVALGY DSVGKYIHQP ESYFGAIVGR YGNRIGKGKF KLEGKEYKLA
     TNNGPNHLHG GLKGFGAHEW DPQKLNDSTL ELTYLSQDQE EGYPGKLLAK VTYTLIGDST
     NCLKIDYEAT TDKPTVVNLT NHTYFNLNGQ GNGTINNHVL QLNAARYTPV DSTLIPTGKL
     EPVAGTPFDF TKPTAIGARI DSPNQQLKFG KGYDYNFVLN PGKGSGLNLA ATVLGDQSDI
     FMEVLTDQPG IQFYGGNFMN GSNPLKGGKK DDHRTAFCLE TQHFPDSPNE PSFPSTELKP
     GQQYKTTTVY RFSVKK
//
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