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Database: UniProt
Entry: A0A0S9CBN7_9SPHN
LinkDB: A0A0S9CBN7_9SPHN
Original site: A0A0S9CBN7_9SPHN 
ID   A0A0S9CBN7_9SPHN        Unreviewed;       378 AA.
AC   A0A0S9CBN7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN   ORFNames=ASE95_12600 {ECO:0000313|EMBL:KQN91080.1};
OS   Sphingomonas sp. Leaf231.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736301 {ECO:0000313|EMBL:KQN91080.1, ECO:0000313|Proteomes:UP000051427};
RN   [1] {ECO:0000313|EMBL:KQN91080.1, ECO:0000313|Proteomes:UP000051427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf231 {ECO:0000313|EMBL:KQN91080.1,
RC   ECO:0000313|Proteomes:UP000051427};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN91080.1, ECO:0000313|Proteomes:UP000051427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf231 {ECO:0000313|EMBL:KQN91080.1,
RC   ECO:0000313|Proteomes:UP000051427};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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|PIRNR:PIRNR005096};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000256|ARBA:ARBA00005028, ECO:0000256|PIRNR:PIRNR005096}.
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:KQN91080.1}.
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DR   EMBL; LMLS01000003; KQN91080.1; -; Genomic_DNA.
DR   RefSeq; WP_056636673.1; NZ_LMLS01000003.1.
DR   AlphaFoldDB; A0A0S9CBN7; -.
DR   STRING; 1736301.ASE95_12600; -.
DR   OrthoDB; 9779408at2; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000051427; 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:SF50; ALDOSE 1-EPIMERASE; 1.
DR   PANTHER; PTHR10091; ALDOSE-1-EPIMERASE; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051427};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..378
FT                   /note="Aldose 1-epimerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006650950"
FT   ACT_SITE        202
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        342
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         102..103
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         276
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   378 AA;  39786 MW;  A7EC16AFD8BC1824 CRC64;
     MRWVMGAGFA LTTGLTCSAA HAATAQRAAF GTLPDGTAVE AVTLTGNNGV SARIMTLGAT
     LQSFNAPDRE GKVADITLGY DDAASYVTAP NFWGQTVGRY ANRIAGGKFA IDGKAYQLPL
     NDKTNSLHGG TKGLDKAVWR ITAVKSGPQA SVTMVTTSPS GDQGYPGKLE VSATYSLDDK
     GALTIDMDAK TDAPTVVNLT NHALFDLAGE GSSGGIYAQR MTIPAARYTP VNAALIPTGE
     LAPVAGTVFD FTKPRAIGQS VRDGRDPQIA IGRGYDHNFV LDKGATKDAQ LAARVEDPTS
     GRVLEVLTTE PGVQFYSGNF LVGALVGKQG HVYRMGDGFA LEPQKFPNTP NQPSFGSARV
     DPGKPYHHRM VYRVSVAR
//
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