ID A0A173X4R1_9BACE Unreviewed; 379 AA.
AC A0A173X4R1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 Name=mro_1 {ECO:0000313|EMBL:CUN45398.1};
GN ORFNames=ERS852397_00258 {ECO:0000313|EMBL:CUN45398.1};
OS Bacteroides finegoldii.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=338188 {ECO:0000313|EMBL:CUN45398.1, ECO:0000313|Proteomes:UP000095517};
RN [1] {ECO:0000313|EMBL:CUN45398.1, ECO:0000313|Proteomes:UP000095517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608840 {ECO:0000313|EMBL:CUN45398.1,
RC ECO:0000313|Proteomes:UP000095517};
RG Pathogen Informatics;
RL Submitted (SEP-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|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; CYZH01000001; CUN45398.1; -; Genomic_DNA.
DR RefSeq; WP_055278279.1; NZ_JADNEP010000021.1.
DR AlphaFoldDB; A0A173X4R1; -.
DR STRING; 338188.ERS852397_00258; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000095517; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000095517};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..379
FT /note="Aldose 1-epimerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008015184"
FT ACT_SITE 205
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 108..109
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 205..207
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 379 AA; 41815 MW; DDBD014D686D0EE5 CRC64;
MKKHFLLAGF AALMLFACNN KPVSELTLSG LDPAKFQTEV NNTQTNLYTL KNKAGMEVCI
TNFGGRIVSI MVPDKNGKMQ DVVLGFDSIA DYINVPSDFG ASIGRYANRI NQGRFVLDGD
TIQLPQNNFG HCLHGGPKGW QYQVYEANLI DPMTLELTRI SPDGDENFPG NVTAKVTYTL
TEDNAIDIKY SATTDKKTII NMTNHSYFNL AGNPSKASTD NILYVNADYY TPVDSTFMTT
GEIAPVKDTP MDFTTPKTVG QDISNYDFVQ LKNGNGYDHN WVLNTKGDIS QVAAKLTSPE
SGITLEVYTN EPGIQVYTGN FLDGTVTGKK GIVYNQRASV CLETQHYPDS PNKVDWPSVV
LEPGQTYNSE CIFKFSVEK
//
