GALE_MYCS2
ID GALE_MYCS2 Reviewed; 313 AA.
AC A0R5C5;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=UDP-glucose 4-epimerase;
DE EC=5.1.3.2;
DE AltName: Full=UDP-galactose 4-epimerase;
DE AltName: Full=Uridine diphosphate galactose 4-epimerase;
GN OrderedLocusNames=MSMEG_6142, MSMEI_5983;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=16381882; DOI=10.1093/nar/gkj060;
RA Perrodou E., Deshayes C., Muller J., Schaeffer C., Van Dorsselaer A.,
RA Ripp R., Poch O., Reyrat J.M., Lecompte O.;
RT "ICDS database: interrupted CoDing sequences in prokaryotic genomes.";
RL Nucleic Acids Res. 34:D338-D343(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [5]
RP PROTEIN SEQUENCE OF 1-26, AND FUNCTION.
RX PubMed=9692181; DOI=10.1016/s0962-8479(98)80005-1;
RA Weston A., Stern R.J., Lee R.E., Nassau P.M., Monsey D., Martin S.L.,
RA Scherman M.S., Besra G.S., Duncan K., McNeil M.R.;
RT "Biosynthetic origin of mycobacterial cell wall galactofuranosyl
RT residues.";
RL Tuber. Lung Dis. 78:123-131(1997).
CC -!- FUNCTION: Involved in the metabolism of galactose. Catalyzes the
CC conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through
CC a mechanism involving the transient reduction of NAD.
CC {ECO:0000269|PubMed:9692181}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose;
CC Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914;
CC EC=5.1.3.2;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK73226.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AFP42416.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK73226.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001663; AFP42416.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_890363.1; NC_008596.1.
DR AlphaFoldDB; A0R5C5; -.
DR SMR; A0R5C5; -.
DR STRING; 246196.MSMEI_5983; -.
DR PRIDE; A0R5C5; -.
DR EnsemblBacteria; ABK73226; ABK73226; MSMEG_6142.
DR EnsemblBacteria; AFP42416; AFP42416; MSMEI_5983.
DR KEGG; msg:MSMEI_5983; -.
DR KEGG; msm:MSMEG_6142; -.
DR PATRIC; fig|246196.19.peg.5981; -.
DR eggNOG; COG0451; Bacteria.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Galactose metabolism;
KW Isomerase; NAD; Reference proteome.
FT CHAIN 1..313
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000420763"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 31..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 56..57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 77..81
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189..190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204..206
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 271..274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 313 AA; 33217 MW; 4D8A32C3108F3CCE CRC64;
MRTLVTGAAG FIGSTLVDRL LADGHGVVGL DDLSSGRAEN LHSAENSDKF EFVKADIVDA
DLTGLLAEFK PEVIFHLAAQ ISVKRSVDDP PFDATVNVVG TVRLAEAARL AGVRKVVHTS
SGGSVYGTPP AYPTSEDMPV NPASPYAAGK VAGEVYLNMY RNLYDLDCSH IAPANVYGPR
QDPHGEAGVV AIFSEALLAG RTTKIFGDGS DTRDYVFVDD VVDAFVRAGG PAGGGQRFNV
GTGVETSTRE LHTAIAGAVG APDEPEFHPP RLGDLRRSRL DNTRAREVLG WQPQVALAEG
IAKTVEFFRN KSQ
