ID   B2IRE8_STRPS            Unreviewed;       345 AA.
AC   B2IRE8;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=galM {ECO:0000313|EMBL:ACB89319.1};
GN   OrderedLocusNames=SPCG_0067 {ECO:0000313|EMBL:ACB89319.1};
OS   Streptococcus pneumoniae (strain CGSP14).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=516950 {ECO:0000313|EMBL:ACB89319.1, ECO:0000313|Proteomes:UP000001682};
RN   [1] {ECO:0000313|EMBL:ACB89319.1, ECO:0000313|Proteomes:UP000001682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGSP14 {ECO:0000313|EMBL:ACB89319.1,
RC   ECO:0000313|Proteomes:UP000001682};
RX   PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA   Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT   "Genome evolution driven by host adaptations results in a more virulent and
RT   antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL   BMC Genomics 10:158-158(2009).
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   -!- 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; CP001033; ACB89319.1; -; Genomic_DNA.
DR   RefSeq; WP_000649422.1; NC_010582.1.
DR   AlphaFoldDB; B2IRE8; -.
DR   KEGG; spw:SPCG_0067; -.
DR   HOGENOM; CLU_031753_1_1_9; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000001682; 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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR005096};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096}.
FT   ACT_SITE        177
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        310
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         177..179
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         249
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   345 AA;  37766 MW;  4C4D93A872C9F2BA CRC64;
     MKAYTERVFG NVEGEDVLAY RFETDGGYQL EVMTYGATIL RYVAPDKAGN FANVILGFDD
     FDSYVGNSPK HGASVGPVAG RIAGATFELN GKTYDLEVNN ASNCNHSGST GWDSSLFEVE
     EVSDHGLTLY TERTDGTGGF PGNLKIWISY HLEETGAYEI SYKVTTDQDT LVNPTNHSYF
     NLSGDFTQTI DRHVFQLNTE GIYSIAPDGV PAKTPEANRD VVKHIYNGAL LKDIFAEEDE
     QIQLASGLDH PFALPAGHDN AGFLYDQNSG RFLLFKTEAP CFVVYTANFV DESVIIGGQP
     MLQHNGIALE AQALPDAIHS DLKGQVILKA GQTFTSKTRY ELVVK
//