ID   A9V079_MONBE            Unreviewed;       410 AA.
AC   A9V079;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
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=MONBRDRAFT_8499 {ECO:0000313|EMBL:EDQ88964.1};
OS   Monosiga brevicollis (Choanoflagellate).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX   NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ88964.1, ECO:0000313|Proteomes:UP000001357};
RN   [1] {ECO:0000313|EMBL:EDQ88964.1, ECO:0000313|Proteomes:UP000001357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX   PubMed=18273011; DOI=10.1038/nature06617;
RG   JGI Sequencing;
RA   King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA   Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA   Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA   Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA   Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA   McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT   "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT   metazoans.";
RL   Nature 451:783-788(2008).
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; CH991552; EDQ88964.1; -; Genomic_DNA.
DR   RefSeq; XP_001746069.1; XM_001746017.1.
DR   AlphaFoldDB; A9V079; -.
DR   STRING; 81824.A9V079; -.
DR   EnsemblProtists; EDQ88964; EDQ88964; MONBRDRAFT_8499.
DR   GeneID; 5891485; -.
DR   KEGG; mbr:MONBRDRAFT_8499; -.
DR   eggNOG; KOG1604; Eukaryota.
DR   InParanoid; A9V079; -.
DR   OMA; ESWKCCA; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000001357; Unassembled WGS sequence.
DR   GO; GO:0004034; F:aldose 1-epimerase activity; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IBA:GO_Central.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
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; 2.
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:UP000001357}.
FT   ACT_SITE        179
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        308
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         83..84
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         179..181
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
SQ   SEQUENCE   410 AA;  45309 MW;  297A416150A614C3 CRC64;
     MAQVEKAEYG KLSETGETVH IYTLTGAQGL VVKIMDYGAT IVSLLAPDES GAKADVVLGF
     ATLADWETKN VPYFGAVIGR VANRIAKGEM EVDGKTYTLA INNGPNHLHG GLRGFDKQVW
     QSEIVENGVR FSLISPDGQE NYPGECKVQV TYTVSEDNKL TLSYEFEVDK RCPVNITNHA
     YFNLAGAASG SVRDHKLTMP STHVTEAIEL IPTGKLLPVE IERGYDVNFV VQREDDSGLC
     LAAEYVSAAM SPFTSMPVFC FVWAFRLRLR DNPHMECGRG IAWLIPNRDV ACGASRLPYN
     PYQAFCLETQ HFPDSVHRPE FPTVLREAGR KYTSQTVYEF YATSSDATSA KKAKTRTSLS
     QERRTLCLLF SGHQGVPCQL SYLQRKPVTG VYLKPTDDER TGQCMSAKAG
//