ID C9KQT4_9FIRM Unreviewed; 371 AA.
AC C9KQT4;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=MITSMUL_05636 {ECO:0000313|EMBL:EEX67766.1};
OS Mitsuokella multacida DSM 20544.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Mitsuokella.
OX NCBI_TaxID=500635 {ECO:0000313|EMBL:EEX67766.1, ECO:0000313|Proteomes:UP000003671};
RN [1] {ECO:0000313|EMBL:EEX67766.1, ECO:0000313|Proteomes:UP000003671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20544 {ECO:0000313|EMBL:EEX67766.1,
RC ECO:0000313|Proteomes:UP000003671};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEX67766.1}.
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DR EMBL; ABWK02000027; EEX67766.1; -; Genomic_DNA.
DR RefSeq; WP_005843081.1; NZ_GG697144.2.
DR AlphaFoldDB; C9KQT4; -.
DR STRING; 500635.MITSMUL_05636; -.
DR GeneID; 78515750; -.
DR PATRIC; fig|500635.8.peg.2223; -.
DR eggNOG; COG2017; Bacteria.
DR HOGENOM; CLU_031753_2_0_9; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000003671; Unassembled WGS sequence.
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 335
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT BINDING 81..82
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 371 AA; 40926 MW; 25CB3CF043E4B360 CRC64;
MATIKKESFG KLSDGREVEL YTLRNTKGTE VKVTTYGARL VAWSAYGKDH KRTDIVLGYA
DGAAYEKDNT SMGGLVGRHA NRIAGGKVTI DGKTYQLDLN TGSHNQNHIH GGFQGFHQKL
WTAEETDQGV KFTYHAADGE GGYPGNMTVH VLYSLSNDNE LSIRYEAVSD ADTVCNLTNH
AYFNLNGFAS GPVLDQKIQI FADKYTWADA ESLPDGRILD VAGTPMDLRQ PTRIGEHIDD
DFDELVMGHG YDHNWVIRDE KPAVETKPSD PSCPIDYVGG GLKKAAYAES DQSGFTLTCY
TTQPGVQFYT GNYLNGGLPG KDGVEFQRRT GFCLETQYFP NAFANPNFPQ PILKKGDTWK
AQTVYVLGQK D
//
