ID   W0EV88_9BACT            Unreviewed;       369 AA.
AC   W0EV88;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|ARBA:ARBA00014165, ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|ARBA:ARBA00013185, ECO:0000256|PIRNR:PIRNR005096};
GN   ORFNames=BARVI_10645 {ECO:0000313|EMBL:AHF13129.1};
OS   Barnesiella viscericola DSM 18177.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae;
OC   Barnesiella.
OX   NCBI_TaxID=880074 {ECO:0000313|EMBL:AHF13129.1, ECO:0000313|Proteomes:UP000018901};
RN   [1] {ECO:0000313|EMBL:AHF13129.1, ECO:0000313|Proteomes:UP000018901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18177 {ECO:0000313|Proteomes:UP000018901};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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   -!- SIMILARITY: Belongs to the aldose epimerase family.
CC       {ECO:0000256|ARBA:ARBA00006206, ECO:0000256|PIRNR:PIRNR005096}.
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DR   EMBL; CP007034; AHF13129.1; -; Genomic_DNA.
DR   RefSeq; WP_025279182.1; NZ_CP007034.1.
DR   AlphaFoldDB; W0EV88; -.
DR   STRING; 880074.BARVI_10645; -.
DR   KEGG; bvs:BARVI_10645; -.
DR   PATRIC; fig|880074.11.peg.2207; -.
DR   eggNOG; COG2017; Bacteria.
DR   HOGENOM; CLU_031753_2_0_10; -.
DR   OrthoDB; 9779408at2; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000018901; Chromosome.
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.
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   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096}.
FT   ACT_SITE        200
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        334
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         200..202
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         272
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   369 AA;  40837 MW;  398C8098C76B12B6 CRC64;
     MKHIIYFAAA LIMVGCASNQ KTTLSGLDKN DFDTIVNNQK ISLFTLHNGD MEVCVTNYGG
     RIVSLMVPDK DGRPRDVVLG HDNIRDYLEI DGNFGAIIGR YGNRINRGRF TLDSIVYQLP
     QNNYGHCLHG GPIGFHHSIW SATQTTDTTL VLTLHSTDGD AGFPGNLNVE VVYSLTSDCG
     LKIAYTAYTN KPTIINLTNH SYFNLSGDHT KEITDELLTI KASGFTPIDS TFMPTGEIRS
     VKGTIFDFNH MHAIGENINA DDEQIINGMG YDHNFVLDKS CPFAAQLYDT VSGIVMTVST
     DQPGLQFYSG NFLDGQVCGK NGIAYPKRSA LCLETQHYPD SPNHLDWPSV RLNPGEKYHT
     ETVYSFSIR
//