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Database: UniProt
Entry: P0A9C3
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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   11-JUN-2014, entry version 78.
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; Enterobacteriales;
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
RT   operon 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.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to 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.,
RA   Mau B., 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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It
CC       is active on D-glucose, L-arabinose, D-xylose, D-galactose,
CC       maltose and lactose.
CC   -!- CATALYTIC ACTIVITY: Alpha-D-glucose = beta-D-glucose.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the aldose epimerase family.
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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; YP_489029.1; NC_007779.1.
DR   ProteinModelPortal; P0A9C3; -.
DR   DIP; DIP-35901N; -.
DR   IntAct; P0A9C3; 4.
DR   MINT; MINT-1249454; -.
DR   STRING; 511145.b0756; -.
DR   SWISS-2DPAGE; P0A9C3; -.
DR   PaxDb; P0A9C3; -.
DR   PRIDE; P0A9C3; -.
DR   EnsemblBacteria; AAC73843; AAC73843; b0756.
DR   EnsemblBacteria; BAA35418; BAA35418; BAA35418.
DR   GeneID; 12932716; -.
DR   GeneID; 944943; -.
DR   KEGG; ecj:Y75_p0729; -.
DR   KEGG; eco:b0756; -.
DR   PATRIC; 32116713; VBIEscCol129921_0782.
DR   EchoBASE; EB1649; -.
DR   EcoGene; EG11698; galM.
DR   eggNOG; COG2017; -.
DR   HOGENOM; HOG000072798; -.
DR   KO; K01785; -.
DR   OMA; CPISLTQ; -.
DR   OrthoDB; EOG69WFM5; -.
DR   PhylomeDB; P0A9C3; -.
DR   BioCyc; EcoCyc:ALDOSE1EPIM-MONOMER; -.
DR   BioCyc; ECOL316407:JW0739-MONOMER; -.
DR   BioCyc; MetaCyc:ALDOSE1EPIM-MONOMER; -.
DR   SABIO-RK; P0A9C3; -.
DR   UniPathway; UPA00242; -.
DR   PRO; PR:P0A9C3; -.
DR   Genevestigator; P0A9C3; -.
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   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; Glyco_hydro-type_carb-bd_sub.
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; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Isomerase; Reference proteome.
FT   CHAIN         1    346       Aldose 1-epimerase.
FT                                /FTId=PRO_0000197443.
FT   ACT_SITE    175    175       Proton donor (By similarity).
FT   ACT_SITE    309    309       Proton acceptor (By similarity).
FT   BINDING      79     79       Substrate (By similarity).
FT   BINDING     245    245       Substrate (By similarity).
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
//
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