ID B2URP8_AKKM8 Unreviewed; 319 AA.
AC B2URP8;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=aldose 1-epimerase {ECO:0000256|ARBA:ARBA00013185};
DE EC=5.1.3.3 {ECO:0000256|ARBA:ARBA00013185};
GN OrderedLocusNames=Amuc_1309 {ECO:0000313|EMBL:ACD05133.1};
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD05133.1, ECO:0000313|Proteomes:UP000001031};
RN [1] {ECO:0000313|Proteomes:UP000001031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013
RC / CIP 107961 / Muc {ECO:0000313|Proteomes:UP000001031};
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(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 -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000256|ARBA:ARBA00005028}.
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}.
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DR EMBL; CP001071; ACD05133.1; -; Genomic_DNA.
DR RefSeq; WP_012420348.1; NZ_CP071807.1.
DR AlphaFoldDB; B2URP8; -.
DR STRING; 349741.Amuc_1309; -.
DR PaxDb; 349741-Amuc_1309; -.
DR KEGG; amu:Amuc_1309; -.
DR eggNOG; COG2017; Bacteria.
DR HOGENOM; CLU_031753_2_0_0; -.
DR OrthoDB; 9779408at2; -.
DR BioCyc; AMUC349741:G1GBX-1397-MONOMER; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000001031; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ACD05133.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001031}.
FT ACT_SITE 165
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT BINDING 69..70
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 165..167
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 233
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ SEQUENCE 319 AA; 34502 MW; 44101695C29ABAC8 CRC64;
MIFGTLPGGA PVELFELSSD KLTVRISNYG GRIISVVKDG MDMIVGPKHF EDMLKDTCYC
GAICGRVANR IAKGRFSIDG DSRTVAVNNG PNHLHGGIQG FDSKVWQVQE AGRNTLVLTL
HSADGEENYP GNLEVVATYT VVEETLHLRL EAYADAATIV NLTNHAYWNL SGKPTIDSMT
LEIRASAYTP VDATNIPDGR ILPVEGTDFD LRKAALLGER NSAAHPDTAA GLDHNYVLDS
EPGDKIAAIL LDPESRHRLI VATDAPGLQV YTGEYLPQAR QGIALEAQGF PNAVNTPHFP
SVILRPGQSS TRSITWTVR
//
