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Database: UniProt
Entry: A0A327R2Y0_9BACT
LinkDB: A0A327R2Y0_9BACT
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ID   A0A327R2Y0_9BACT        Unreviewed;       389 AA.
AC   A0A327R2Y0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN   ORFNames=LX64_00020 {ECO:0000313|EMBL:RAJ10418.1};
OS   Chitinophaga skermanii.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=331697 {ECO:0000313|EMBL:RAJ10418.1, ECO:0000313|Proteomes:UP000249547};
RN   [1] {ECO:0000313|EMBL:RAJ10418.1, ECO:0000313|Proteomes:UP000249547}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23857 {ECO:0000313|EMBL:RAJ10418.1,
RC   ECO:0000313|Proteomes:UP000249547};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-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   -!- 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}.
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:RAJ10418.1}.
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DR   EMBL; QLLL01000001; RAJ10418.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327R2Y0; -.
DR   OrthoDB; 9779408at2; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000249547; 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; 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; PS51257; PROKAR_LIPOPROTEIN; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249547};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..389
FT                   /note="Aldose 1-epimerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016363448"
FT   ACT_SITE        217
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        354
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         120..121
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         289
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   389 AA;  43351 MW;  54D1F15BA50BBB8F CRC64;
     MLKSAAYCLV LMSVVFMSCE TGKNKQTQAD SARASDSAKL FLVERDFDTT IGTNKVSLFY
     LQNSHGTRMA VTNYGAKVVA LSVPDRNGKF EDIVLGFSNI DKYFEPHEKY YGGVVGRYAN
     RIGDSKFKIN DTIFPLYANN GLNNLHGGKS GFNAVVWEVS QPDSQNLVFH YRSYDGEEGF
     PGNLDVNMVY TLTENNTFRI HYTATTDKAT HVNLSHHSFF NLKGAGNGPI TDHILMINAN
     AYTPIKEDLI PTGEIAPVAN TPLDFTTPRA IGEHLDTTND QIRKGKGYDH NWVLNNNKGN
     LALAASILEP KSGRYMEVWT TEPGIQFYSG NFLGGADTGK FNKPYKFREA FCLETQHFPN
     SPNQPNFPST LLLPGKTYSQ SCEYRFSTK
//
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