ID F2JML1_CELLD Unreviewed; 348 AA.
AC F2JML1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=Clole_2965 {ECO:0000313|EMBL:ADZ84662.1};
OS Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS RHM5) (Clostridium lentocellum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC Cellulosilyticum.
OX NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ84662.1, ECO:0000313|Proteomes:UP000008467};
RN [1] {ECO:0000313|EMBL:ADZ84662.1, ECO:0000313|Proteomes:UP000008467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC {ECO:0000313|Proteomes:UP000008467};
RX PubMed=21398547; DOI=10.1128/JB.00239-11;
RG US DOE Joint Genome Institute;
RA Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA Angert E.R., Currie C.R.;
RT "Complete genome sequence of the cellulose-degrading bacterium
RT Cellulosilyticum lentocellum.";
RL J. Bacteriol. 193:2357-2358(2011).
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; CP002582; ADZ84662.1; -; Genomic_DNA.
DR RefSeq; WP_013657942.1; NC_015275.1.
DR AlphaFoldDB; F2JML1; -.
DR STRING; 642492.Clole_2965; -.
DR KEGG; cle:Clole_2965; -.
DR eggNOG; COG2017; Bacteria.
DR HOGENOM; CLU_031753_1_1_9; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000008467; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008467}.
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT BINDING 179..181
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 252
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ SEQUENCE 348 AA; 39027 MW; F551F50A40777FEE CRC64;
MKIVSKDMTF ASGEKVTKYE LSNTAGMTVE VLNWGATLTK IVVPDKEGHF ENVILEWEDI
NTYENNPGNF GATVGRIAGR IADAKVTLNH QVYHFVKNTY GNTLHGGLVG FDKKAWTGEM
QQTEDSVILT LSYLSPDGEE GFPGNLHVKA IYLLKEDNTL TLTYEATTDK ETIVNLTNHA
YFNLSGEAKR SVLGQEVYIN SSQICDLNEE LIPTGAFIDL DNESAFDFRV PKAIGKDIER
ENPHLKNGYG YDHCWLLNKG EKAAELYDPI SGRVMEISTT APGVVVYTMN HADGVTKLSN
GKEQQRRYGV CFETQRKPIG KNEVFKEEVI LKPSEVYRQE TTFKFSNR
//
