ID D5VJF9_CAUST Unreviewed; 379 AA.
AC D5VJF9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN OrderedLocusNames=Cseg_1895 {ECO:0000313|EMBL:ADG10368.1};
OS Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 /
OS LMG 17158 / TK0059) (Mycoplana segnis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=509190 {ECO:0000313|EMBL:ADG10368.1, ECO:0000313|Proteomes:UP000002629};
RN [1] {ECO:0000313|Proteomes:UP000002629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 /
RC TK0059 {ECO:0000313|Proteomes:UP000002629};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(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|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}.
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DR EMBL; CP002008; ADG10368.1; -; Genomic_DNA.
DR RefSeq; WP_013079024.1; NC_014100.1.
DR AlphaFoldDB; D5VJF9; -.
DR STRING; 509190.Cseg_1895; -.
DR KEGG; cse:Cseg_1895; -.
DR eggNOG; COG2017; Bacteria.
DR HOGENOM; CLU_031753_2_0_5; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000002629; 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; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..379
FT /note="Aldose 1-epimerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003078905"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT ACT_SITE 343
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 277
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ SEQUENCE 379 AA; 39649 MW; 8CD8D0ED521AB250 CRC64;
MTLKTIALYG ALALAATSTA TAAELSRRPF GQTPSGEAVE AVTLTNAKGV SATVITYGAT
LQSLVAPDKA GKKADIVLGF NDAATYVKNA SYFGATVGRF ANRIGKGRFE LDGKTYQLAL
NNNGVAALHG GVKGFDKVVW KVLETKSGPT ASVTLGYVSP DGDQGYPGTV NATATYALDE
QNQLTITYGA TTDKPTIVNM TNHALFNVAG EGSPDGAMGN LLTIPADGYT PVDNELIPTG
ATTPVAGTAF DFRTPTAVGA RIRDASEPQL IVGKGYDHNY VLNGKSGGAL RLAARLADPK
SGRVLEILSD QPGVQFYAGN FLDGSWIGKS GKLYRQGDGI ALEPQHFPDA PNKPQFAPVR
LDPGQTYRNV MIFKVGVAK
//
