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Database: UniProt
Entry: I0Z1W3_COCSC
LinkDB: I0Z1W3_COCSC
Original site: I0Z1W3_COCSC 
ID   I0Z1W3_COCSC            Unreviewed;       341 AA.
AC   I0Z1W3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN   ORFNames=COCSUDRAFT_36007 {ECO:0000313|EMBL:EIE24632.1};
OS   Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC   Coccomyxa subellipsoidea.
OX   NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE24632.1, ECO:0000313|Proteomes:UP000007264};
RN   [1] {ECO:0000313|EMBL:EIE24632.1, ECO:0000313|Proteomes:UP000007264}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-169 {ECO:0000313|EMBL:EIE24632.1,
RC   ECO:0000313|Proteomes:UP000007264};
RX   PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA   Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA   Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA   Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA   Van Etten J., Lomsadze A., Borodovsky M.;
RT   "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT   reveals traits of cold adaptation.";
RL   Genome Biol. 13:R39-R39(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|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:EIE24632.1}.
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DR   EMBL; AGSI01000005; EIE24632.1; -; Genomic_DNA.
DR   RefSeq; XP_005649176.1; XM_005649119.1.
DR   AlphaFoldDB; I0Z1W3; -.
DR   STRING; 574566.I0Z1W3; -.
DR   GeneID; 17042634; -.
DR   KEGG; csl:COCSUDRAFT_36007; -.
DR   eggNOG; KOG1604; Eukaryota.
DR   OrthoDB; 334899at2759; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000007264; 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; 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.
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:UP000007264}.
FT   ACT_SITE        163
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        306
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         63..64
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         163..165
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         229
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   341 AA;  36863 MW;  D0CFD73722C4B549 CRC64;
     MHVLQGPDGM EVHISPLGGV IQRLYVPDVE GNLEDVVLGF DDMAPYADGT SPYFGAVVGR
     VANRIAKGIF SLEGRTYKLT VNNGPNALHG GKRGFDKVIW QGARISHPEG DALRLTYTSR
     DGEEGYPGTL IATLTYIMTR EGMLKVIFEA TADKQTPVNI VQHSYFNLAG HASGSALDHT
     LYINGDHYTP LDETAIPTGE IAPVAGTPFD FSDEHSIGES IGQVSGGYDH NYVLFGMGRQ
     AKFIVKNGAA SNKPKLAAKL TDPKSRRCLK VLTTAPGMQF YSGNFLEGIR GKDGAVYNKH
     AGVCLETQGF PNAVNEHAFP SVILGPGEKY RHEVDYQFSN A
//
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