ID D8GI27_CLOLD Unreviewed; 353 AA.
AC D8GI27;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Aldose 1-epimerase {ECO:0000256|ARBA:ARBA00013185, ECO:0000256|PIRNR:PIRNR005096};
DE EC=5.1.3.3 {ECO:0000256|ARBA:ARBA00013185, ECO:0000256|PIRNR:PIRNR005096};
GN OrderedLocusNames=CLJU_c18270 {ECO:0000313|EMBL:ADK14889.1};
OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK14889.1, ECO:0000313|Proteomes:UP000001656};
RN [1] {ECO:0000313|EMBL:ADK14889.1, ECO:0000313|Proteomes:UP000001656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55383 / DSM 13528 / PETC
RC {ECO:0000313|Proteomes:UP000001656};
RX PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT "Clostridium ljungdahlii represents a microbial production platform based
RT on syngas.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the aldose epimerase family.
CC {ECO:0000256|ARBA:ARBA00006206, ECO:0000256|PIRNR:PIRNR005096}.
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DR EMBL; CP001666; ADK14889.1; -; Genomic_DNA.
DR RefSeq; WP_013238481.1; NZ_LITS01000007.1.
DR AlphaFoldDB; D8GI27; -.
DR STRING; 748727.CLJU_c18270; -.
DR KEGG; clj:CLJU_c18270; -.
DR PATRIC; fig|748727.19.peg.3432; -.
DR eggNOG; COG2017; Bacteria.
DR HOGENOM; CLU_031753_1_1_9; -.
DR OrthoDB; 9779408at2; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000001656; 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; ALDOSE-1-EPIMERASE; 1.
DR PANTHER; PTHR10091:SF0; GALACTOSE MUTAROTASE; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT ACT_SITE 181
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT BINDING 80..81
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 181..183
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 253
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ SEQUENCE 353 AA; 40116 MW; F2CE295449811621 CRC64;
MGIMKEVFGK VSKDKEVYIF TLCNENSMSV KISNYGGRLI SLTVPDKEGK LDDIVLGYKN
LEGYIKGKFF FGAIIGRNAN RIKGAEIKID DKVYSLTKNE GENQLHGGIV GFDKVLWTPR
TYVDDDGNEC LELLYTSKDG EEGYPGNLNV KVVYTIKRDN ELRIDYFAVS DKDTVVNLTN
HSYFNLSGHL SKSILDHQVM INSDRFTAND RESVPTGEIR FVENTPMDFR KLTTVGKSIS
SKYDQIIYGN GYDHNWILNR KGKNLEMAAE VLDPRSGRVM KVYTTKPGVQ FYTGNYLNEF
ENCKGDTCYT KNSGLCLETQ YFPDALNHNN FPSPVLKVGE NYRHTTIYKF LTI
//
