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Database: UniProt
Entry: H2JF73_9CLOT
LinkDB: H2JF73_9CLOT
Original site: H2JF73_9CLOT 
ID   H2JF73_9CLOT            Unreviewed;       354 AA.
AC   H2JF73;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
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   ORFNames=Clo1100_1202 {ECO:0000313|EMBL:AEY65453.1};
OS   Clostridium sp. BNL1100.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=755731 {ECO:0000313|EMBL:AEY65453.1, ECO:0000313|Proteomes:UP000007324};
RN   [1] {ECO:0000313|EMBL:AEY65453.1, ECO:0000313|Proteomes:UP000007324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNL1100 {ECO:0000313|EMBL:AEY65453.1,
RC   ECO:0000313|Proteomes:UP000007324};
RX   PubMed=23209234; DOI=10.1128/JB.01908-12;
RA   Li L.L., Taghavi S., Izquierdo J.A., van der Lelie D.;
RT   "Complete Genome Sequence of Clostridium sp. Strain BNL1100, a Cellulolytic
RT   Mesophile Isolated from Corn Stover.";
RL   J. Bacteriol. 194:6982-6983(2012).
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; CP003259; AEY65453.1; -; Genomic_DNA.
DR   RefSeq; WP_014312835.1; NC_016791.1.
DR   AlphaFoldDB; H2JF73; -.
DR   STRING; 755731.Clo1100_1202; -.
DR   KEGG; clb:Clo1100_1202; -.
DR   PATRIC; fig|755731.4.peg.1198; -.
DR   eggNOG; COG2017; Bacteria.
DR   HOGENOM; CLU_031753_1_1_9; -.
DR   OrthoDB; 9779408at2; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000007324; 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        180
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        319
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         180..182
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   354 AA;  39764 MW;  0A86D3CC2B412788 CRC64;
     MSITKKNFAK MPDGTQVDIY TLKNSNNMSI DILNYGGTIV SILMPDKNGK IADIALGFDD
     IKRYMENDAY MGALIGRHGN RIEGAEFELN GKVYELVKND GNNHLHGGTI GFHNVVWNAE
     IQEEKGVQKL VLTHTSPDGE ENYPGNLNVK VEYSLSENNE LKIDYNAVSD KDTVVNLTNH
     AYFNLSGHDS GDVLKHQIYI NADKFTPVND ECIPTGEIRD VKGTVMDFTK LSSFSEGISS
     GDEQIVYGLG YDHNWVLNTE GNINEVACEL YEPESGRAMQ VFTTKPGIQF YSGNHLNEKV
     ELIGKNNTVY NKRTGLCLET QFFPNAMKHK NFPSPILKAN ETYHYVTIYK FFNK
//
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