GALE_MYCTU
ID GALE_MYCTU Reviewed; 314 AA.
AC P9WN67; F2GF05; L0TES1; Q6MWV3; Q7D561;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
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 Name=galE1; OrderedLocusNames=Rv3634c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 (By similarity).
CC {ECO:0000250}.
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}.
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DR EMBL; AL123456; CCP46457.1; -; Genomic_DNA.
DR PIR; C70562; C70562.
DR RefSeq; NP_215015.2; NC_000962.3.
DR RefSeq; WP_003419610.1; NZ_NVQJ01000045.1.
DR PDB; 6LTT; X-ray; 1.97 A; A/B=1-314.
DR PDBsum; 6LTT; -.
DR AlphaFoldDB; P9WN67; -.
DR SMR; P9WN67; -.
DR STRING; 83332.Rv3634c; -.
DR PaxDb; P9WN67; -.
DR DNASU; 885765; -.
DR GeneID; 885765; -.
DR KEGG; mtu:Rv3634c; -.
DR TubercuList; Rv3634c; -.
DR eggNOG; COG0451; Bacteria.
DR OMA; EPIKVFN; -.
DR PhylomeDB; P9WN67; -.
DR BioCyc; MetaCyc:G185E-7913-MON; -.
DR BRENDA; 5.1.3.2; 3445.
DR UniPathway; UPA00214; -.
DR PRO; PR:P9WN67; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 3D-structure; Carbohydrate metabolism; Galactose metabolism; Isomerase;
KW NAD; Reference proteome.
FT CHAIN 1..314
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000420762"
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"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6LTT"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:6LTT"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:6LTT"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:6LTT"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6LTT"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6LTT"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6LTT"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:6LTT"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:6LTT"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:6LTT"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:6LTT"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:6LTT"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:6LTT"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:6LTT"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6LTT"
FT TURN 122..126
FT /evidence="ECO:0007829|PDB:6LTT"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:6LTT"
FT HELIX 145..164
FT /evidence="ECO:0007829|PDB:6LTT"
FT STRAND 167..178
FT /evidence="ECO:0007829|PDB:6LTT"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:6LTT"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:6LTT"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:6LTT"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6LTT"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:6LTT"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:6LTT"
FT HELIX 248..259
FT /evidence="ECO:0007829|PDB:6LTT"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6LTT"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:6LTT"
FT HELIX 297..310
FT /evidence="ECO:0007829|PDB:6LTT"
SQ SEQUENCE 314 AA; 33582 MW; EED55D1C848C6B67 CRC64;
MRALVTGAAG FIGSTLVDRL LADGHSVVGL DNFATGRATN LEHLADNSAH VFVEADIVTA
DLHAILEQHR PEVVFHLAAQ IDVRRSVADP QFDAAVNVIG TVRLAEAARQ TGVRKIVHTS
SGGSIYGTPP EYPTPETAPT DPASPYAAGK VAGEIYLNTF RHLYGLDCSH IAPANVYGPR
QDPHGEAGVV AIFAQALLSG KPTRVFGDGT NTRDYVFVDD VVDAFVRVSA DVGGGLRFNI
GTGKETSDRQ LHSAVAAAVG GPDDPEFHPP RLGDLKRSCL DIGLAERVLG WRPQIELADG
VRRTVEYFRH KHTD
