ID W0EM79_9BACT Unreviewed; 378 AA.
AC W0EM79;
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_02945 {ECO:0000313|EMBL:AHF11955.1}, BARVI_06000
GN {ECO:0000313|EMBL:AHF12403.1};
OS Barnesiella viscericola DSM 18177.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae;
OC Barnesiella.
OX NCBI_TaxID=880074 {ECO:0000313|EMBL:AHF11955.1, ECO:0000313|Proteomes:UP000018901};
RN [1] {ECO:0000313|EMBL:AHF11955.1, ECO:0000313|Proteomes:UP000018901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C46 {ECO:0000313|EMBL:AHF11955.1}, and DSM 18177
RC {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; AHF11955.1; -; Genomic_DNA.
DR EMBL; CP007034; AHF12403.1; -; Genomic_DNA.
DR RefSeq; WP_025277774.1; NZ_CP007034.1.
DR AlphaFoldDB; W0EM79; -.
DR STRING; 880074.BARVI_02945; -.
DR KEGG; bvs:BARVI_02945; -.
DR KEGG; bvs:BARVI_06000; -.
DR PATRIC; fig|880074.11.peg.1259; -.
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 206
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT BINDING 109..110
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 206..208
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 278
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ SEQUENCE 378 AA; 41502 MW; E7CCBEC310F62807 CRC64;
MNSKLIWAGA WVVLLAACTS KSDTEGVTKS GLDRSKFETT VDGKPVKLYV LENQSGMEVC
VTNYGGRIVS VMVPDRDNQY RDVVLGHDSI ADYIHIDGNF GALIGRYGNR IAQGRFTLDG
VEYQLPQNNY GHCLHGGPKG FHHSVWNAVQ PNDTTLELTL QSPDGEAGFP GNLDVKVVYT
LTSDNALRLQ YTATTDKPTI VNLTNHSYFN LSGNPAHDIL DETVQFCADG FTPIDSTFMT
WGEIRPVEGT PFDFRAGKTV GRDIDADDEQ LKNGMGYDHN MVLSTGGDLS KVACRISDPT
TGIVLEVYTT EPGIQFYTGN FLDGKVKGKR GIAYPRRAAI CVETQHYPDS PNQPNYPSVV
LRPGETYSST CIYKFGVE
//
