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Database: UniProt
Entry: A0A0M8MGL2_9FLAO
LinkDB: A0A0M8MGL2_9FLAO
Original site: A0A0M8MGL2_9FLAO 
ID   A0A0M8MGL2_9FLAO        Unreviewed;       390 AA.
AC   A0A0M8MGL2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN   ORFNames=AM493_07050 {ECO:0000313|EMBL:KOS05821.1};
OS   Flavobacterium akiainvivens.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1202724 {ECO:0000313|EMBL:KOS05821.1, ECO:0000313|Proteomes:UP000037755};
RN   [1] {ECO:0000313|EMBL:KOS05821.1, ECO:0000313|Proteomes:UP000037755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IK-1 {ECO:0000313|EMBL:KOS05821.1,
RC   ECO:0000313|Proteomes:UP000037755};
RA   Wan X., Hou S., Saito J., Donachie S.;
RT   "Whole genome sequence of Flavobacterium akiainvivens IK-1T, from decaying
RT   Wikstroemia oahuensis, an endemic Hawaiian shrub.";
RL   Submitted (AUG-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   -!- 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:KOS05821.1}.
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DR   EMBL; LIYD01000005; KOS05821.1; -; Genomic_DNA.
DR   RefSeq; WP_054407065.1; NZ_LIYD01000005.1.
DR   AlphaFoldDB; A0A0M8MGL2; -.
DR   STRING; 1202724.AM493_07050; -.
DR   PATRIC; fig|1202724.3.peg.1466; -.
DR   OrthoDB; 9779408at2; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000037755; 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:UP000037755};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..390
FT                   /note="Aldose 1-epimerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005818364"
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   390 AA;  42458 MW;  D4F5C6EAF78255E4 CRC64;
     MKKYKSIICC LAGVLVIVSC KNETPANNGN TEKPTTEKQV AELKKADFES TIDGKATGLY
     FIEAKDIKIA FTNYGARIVG LWVPDSKGVM TDVVVGHGSV SDFKNSSEPY FGATIGRVGN
     RIAKGTFKVD GKEYHVPLNN GVNSLHGGKK GFQDVVWDVK QTDAKTLVFS YLSPDGEQGF
     PGNLKVTVTY SVDDNQTLKM DYKATTDAKT PVNLTNHAFF NLNGEGSGTI LNHQVMINAN
     KYTPVDEGLI PFGKLEAVAG TPFDFTTFHT IGERVEAENQ QLKNGAGYDH NYALNTTGKG
     LEKAATVVGD KSGIQMDVYT VEPGLQFYSG NFMKGQNTFK SGAKDDFRTA FAMETQHFPD
     AINQPAFAPI TLEPGAAYHT VSEYRFSVKK
//
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