ID A8AUB1_STRGC Unreviewed; 344 AA. AC A8AUB1; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 85. 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:ABV10531.1}; GN OrderedLocusNames=SGO_0049 {ECO:0000313|EMBL:ABV10531.1}; OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / OS DL1 / V288). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=467705 {ECO:0000313|EMBL:ABV10531.1, ECO:0000313|Proteomes:UP000001131}; RN [1] {ECO:0000313|EMBL:ABV10531.1, ECO:0000313|Proteomes:UP000001131} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288 RC {ECO:0000313|Proteomes:UP000001131}; RX PubMed=17720781; DOI=10.1128/JB.01023-07; RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.; RT "Genome-wide transcriptional changes in Streptococcus gordonii in response RT to competence signaling peptide."; RL J. Bacteriol. 189:7799-7807(2007). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000725; ABV10531.1; -; Genomic_DNA. DR RefSeq; WP_011999600.1; NC_009785.1. DR AlphaFoldDB; A8AUB1; -. DR STRING; 467705.SGO_0049; -. DR KEGG; sgo:SGO_0049; -. DR eggNOG; COG2017; Bacteria. DR HOGENOM; CLU_031753_2_0_9; -. DR UniPathway; UPA00242; -. DR Proteomes; UP000001131; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000001131}. FT ACT_SITE 177 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1" FT ACT_SITE 309 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 248 FT /ligand="beta-D-galactose" FT /ligand_id="ChEBI:CHEBI:27667" FT /evidence="ECO:0000256|PIRSR:PIRSR005096-2" SQ SEQUENCE 344 AA; 38246 MW; 36F1D2DA60ABD1A6 CRC64; MKSYQKTIFG EFQGQNIFRF TFENDLGYRL SVMNYGATIL EYQTPDKKGQ FANVILGFDQ FEDYIGNSPK HGASIGPVAG RIAGASFELG GEIYHLEANN GQNCNHSGST GWDSTVFQVE EVTDEGLVLF TERADGTGGF PGHLKVWISY TLSEKGELEI SYQVQTDRDT LINPTNHSYF NLSADFAQSI DDHVFQVDSL GFYPIAEDGV PAKETEISDF VKHLQQAMLL KDLFAEKDEQ VRLVSGLDHP FALKPGHETA GFLYHQESGR FLTFKTEAPC LVVYTANCVD EAIRFGGQTM KQHNGVALEM QALPDAIHSH QKDQVIVRAG QEFTSTTTYH AIAK //