ID   GALM_STRTR              Reviewed;         348 AA.
AC   P21955;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Aldose 1-epimerase;
DE            EC=5.1.3.3;
DE   AltName: Full=Galactose mutarotase;
DE   AltName: Full=Type-1 mutarotase;
GN   Name=galM;
OS   Streptococcus thermophilus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A147;
RX   PubMed=1694527; DOI=10.1128/jb.172.7.4037-4047.1990;
RA   Poolman B., Royer T.J., Mainzer S.E., Schmidt B.F.;
RT   "Carbohydrate utilization in Streptococcus thermophilus: characterization
RT   of the genes for aldose 1-epimerase (mutarotase) and UDPglucose 4-
RT   epimerase.";
RL   J. Bacteriol. 172:4037-4047(1990).
CC   -!- FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is
CC       active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and
CC       lactose (By similarity). {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU10126};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- SIMILARITY: Belongs to the aldose epimerase family. {ECO:0000305}.
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DR   EMBL; M38175; AAA26945.1; -; Genomic_DNA.
DR   PIR; B44509; B44509.
DR   RefSeq; WP_014608520.1; NZ_VBTK01000009.1.
DR   AlphaFoldDB; P21955; -.
DR   SMR; P21955; -.
DR   STRING; 322159.STER_1368; -.
DR   eggNOG; COG2017; Bacteria.
DR   BioCyc; MetaCyc:MON-6141; -.
DR   UniPathway; UPA00242; -.
DR   GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR018052; Ald1_epimerase_CS.
DR   InterPro; IPR013458; Ald_epimerase_bac.
DR   InterPro; IPR015443; Aldose_1-epimerase.
DR   InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   PIRSF; PIRSF005096; GALM; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   TIGRFAMs; TIGR02636; galM_Leloir; 1.
DR   PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase.
FT   CHAIN           1..348
FT                   /note="Aldose 1-epimerase"
FT                   /id="PRO_0000197447"
FT   ACT_SITE        180
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10126"
FT   ACT_SITE        311
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   348 AA;  39013 MW;  17C3EE027ABE1F92 CRC64;
     MKISCEIIGK VDSGDVSKIS MENNNGVVIS TLTTGATLQE FLVPMETGAL KNIVLGFSDF
     EDYYKNNLCA CQSIGRVAGR IGKASYTHNM VLYSLPKNEG DNCLHGGPKG MQVQNWNYVT
     NLNDDYVETK FIRRLYSSVD GFPGDVTVSI SYRLNNNNRL TILFEAFDVT ESTVFNPTNH
     VYFNLSDKQD LSSHELQIYS DYRLELDSEL IPTGQKINVD ETNYDFRKTT DLLPRIEANN
     GFDDAFVVGG GTCDHVKEVA ILHDKESGDG IEIFSNRNGL VIFTMDDIED NIYFARDKGK
     MAKRREAIAM EAQTLPDAVN HKGFGDIILD KGHSVNYEIG FQYFNSSR