GALM_ECOLI
ID GALM_ECOLI Reviewed; 346 AA.
AC P0A9C3; P40681;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Aldose 1-epimerase;
DE EC=5.1.3.3;
DE AltName: Full=Galactose mutarotase;
DE AltName: Full=Type-1 mutarotase;
GN Name=galM; OrderedLocusNames=b0756, JW0739;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-14.
RC STRAIN=K12 / SA1308;
RX PubMed=7966338; DOI=10.1006/jmbi.1994.1728;
RA Bouffard G.G., Rudd K.E., Adhya S.L.;
RT "Dependence of lactose metabolism upon mutarotase encoded in the gal operon
RT in Escherichia coli.";
RL J. Mol. Biol. 244:269-278(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is
CC active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and
CC lactose.
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:0000255|PROSITE-ProRule:PRU10126};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aldose epimerase family. {ECO:0000305}.
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DR EMBL; U13636; AAB17020.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73843.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35418.1; -; Genomic_DNA.
DR PIR; D64811; D64811.
DR RefSeq; NP_415277.1; NC_000913.3.
DR RefSeq; WP_000931389.1; NZ_STEB01000028.1.
DR AlphaFoldDB; P0A9C3; -.
DR SMR; P0A9C3; -.
DR BioGRID; 4261710; 25.
DR DIP; DIP-35901N; -.
DR IntAct; P0A9C3; 4.
DR STRING; 511145.b0756; -.
DR SWISS-2DPAGE; P0A9C3; -.
DR jPOST; P0A9C3; -.
DR PaxDb; P0A9C3; -.
DR PRIDE; P0A9C3; -.
DR EnsemblBacteria; AAC73843; AAC73843; b0756.
DR EnsemblBacteria; BAA35418; BAA35418; BAA35418.
DR GeneID; 66670973; -.
DR GeneID; 944943; -.
DR KEGG; ecj:JW0739; -.
DR KEGG; eco:b0756; -.
DR PATRIC; fig|1411691.4.peg.1522; -.
DR EchoBASE; EB1649; -.
DR eggNOG; COG2017; Bacteria.
DR HOGENOM; CLU_031753_1_0_6; -.
DR InParanoid; P0A9C3; -.
DR OMA; ATWLSCK; -.
DR PhylomeDB; P0A9C3; -.
DR BioCyc; EcoCyc:ALDOSE1EPIM-MON; -.
DR BioCyc; MetaCyc:ALDOSE1EPIM-MON; -.
DR BRENDA; 5.1.3.3; 2026.
DR SABIO-RK; P0A9C3; -.
DR UniPathway; UPA00242; -.
DR PRO; PR:P0A9C3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0004034; F:aldose 1-epimerase activity; IDA:EcoCyc.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IMP:EcoCyc.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR018052; Ald1_epimerase_CS.
DR InterPro; IPR013458; Ald_epimerase_bac.
DR InterPro; IPR015443; Aldose_1-epimerase.
DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR Pfam; PF01263; Aldose_epim; 1.
DR PIRSF; PIRSF005096; GALM; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR TIGRFAMs; TIGR02636; galM_Leloir; 1.
DR PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Direct protein sequencing; Isomerase;
KW Reference proteome.
FT CHAIN 1..346
FT /note="Aldose 1-epimerase"
FT /id="PRO_0000197443"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10126"
FT ACT_SITE 309
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 38190 MW; 4373732BAEA83E1D CRC64;
MLNETPALAP DGQPYRLLTL RNNAGMVVTL MDWGATLLSA RIPLSDGSVR EALLGCASPE
CYQDQAAFLG ASIGRYANRI ANSRYTFDGE TVTLSPSQGV NQLHGGPEGF DKRRWQIVNQ
NDRQVLFALS SDDGDQGFPG NLGATVQYRL TDDNRISITY RATVDKPCPV NMTNHVYFNL
DGEQSDVRNH KLQILADEYL PVDEGGIPHD GLKSVAGTSF DFRSAKIIAS EFLADDDQRK
VKGYDHAFLL QAKGDGKKVA AHVWSADEKL QLKVYTTAPA LQFYSGNFLG GTPSRGTEPY
ADWQGLALES EFLPDSPNHP EWPQPDCFLR PGEEYSSLTE YQFIAE
