Entry Information
Protein Name GalM
Accession No P0A9C3
Protein description Aldose 1-epimerase
pI/Mw (Da)
Theoretical Experimental
4.84/38190.46 4.97/39311 (4-5)
4.83/39220 (4-5)
Protein function and expression Converts alpha-aldose to the beta-anomer. Active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose.
Reference(s) Lopez-Campistrous, A., P. Semchuk, L. Burke, T. Palmer-Stone, S. J. Brokx, G. Broderick, D. Bottorff, S. Bolch, J. H. Weiner, and M. J. Ellison. 2005. Localization, annotation & comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell. Proteomics 4:1205-1209. (NCBI)

Tonella, L., C. Hoogland, P. A. Binz, R. D. Appel, D. F. Hochstrasser, and J. C. Sanchez. 2001. New perspectives in the Escherichia coli proteome investigation. Proteomics 1:409-423. (NCBI)

Swiss-Prot Database Reference

Entry information
Entry Name GALM_ECOLI
Primary accession number P0A9C3
Secondary accession numbers P40681 
Integrated into Swiss-Prot on 2005-07-19
Sequence was last modified on 2005-07-19 (Sequence version 1)
Annotations were last modified on 2006-09-05 (Entry version 14)
Name and origin of the protein
Protein name Aldose 1-epimerase
Synonyms EC 5.1.3.3 Aldose 1-epimerase
Mutarotase
Gene name Name : galM
OrderedLocusName : b0756
From Escherichia coli [TaxID:562] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia;
References
[1] NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-14.
strain = K12 / SA1308
PubMed=7966338[NCBI, ExPASy, EBI, Israel, Japan]
Bouffard G.G. , Rudd K.E. , Adhya S.L. ,
"Dependence of lactose metabolism upon mutarotase encoded in the gal operon in Escherichia coli."
J. Mol. Biol.244:269-278(1994) 
[2] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
DOI=10.1093/dnares/3.3.137;PubMed=8905232[NCBI, ExPASy, EBI, Israel, Japan]
Oshima T. , Aiba H. , Baba T. , Fujita K. , Hayashi K. , Honjo A. , Ikemoto K. , Inada T. , Itoh T. , Kajihara M. , Kanai K. , Kashimoto K. , Kimura S. , Kitagawa M. , Makino K. , Masuda S. , Miki T. , Mizobuchi K. , Mori H. , Motomura K. , Nakamura Y. , Nashimoto H. , Nishio Y. , Saito N. , Sampei G. , Seki Y. , Tagami H. , Takemoto K. , Wada C. , Yamamoto Y. , Yano M. , Horiuchi T. ,
"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
DNA Res.3:137-155(1996) 
[3] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / MG1655 / ATCC 47076
DOI=10.1126/science.277.5331.1453;PubMed=9278503[NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R. , Plunkett G. III , Bloch C.A. , Perna N.T. , Burland V. , Riley M. , Collado-Vides J. , Glasner J.D. , Rode C.K. , Mayhew G.F. , Gregor J. , Davis N.W. , Kirkpatrick H.A. , Goeden M.A. , Rose D.J. , Mau B. , Shao Y. ,
"The complete genome sequence of Escherichia coli K-12."
Science277:1453-1474(1997) 
[4] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
DOI=10.1038/msb4100049;
Hayashi K. , Morooka N. , Yamamoto Y. , Fujita K. , Isono K. , Choi S. , Ohtsubo E. , Baba T. , Wanner B.L. , Mori H. , Horiuchi T. ,
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Mol. Syst. Biol.2:E1-E5(2006) 
Comments
  • FUNCTION : Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose
  • CATALYTIC ACTIVITY : Alpha-D-glucose = beta-D-glucose
  • PATHWAY : Hexose metabolism
  • SUBCELLULAR LOCATION : Cytoplasm (Probable)
  • SIMILARITY : Belongs to the aldose epimerase family
  • Copyright
    Copyrighted by the UniProt Consortium, see http://www.uniprot.org/. Distributed under the Creative Commons Attribution-NoDerivs License.
    Cross-reference
    Sequence databases
    EMBL U13636;AAB17020.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U00096;AAC73843.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    AP009048;BAA35418.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    PIR D64811;D64811.
    3D structure databases
    ModBase P0A9C3
    Protein-protein interaction databases
    IntAct P0A9C3;-.
    DIP P0A9C3
    Enzyme and pathway databases
    BioCyc EcoCyc:ALDOSE1EPIM-MONOMER;-.
    2D gel databases
    SWISS-2DPAGE P0A9C3;COLI.
    Organism-specific gene databases
    EchoBASE EB1649;-.
    EcoGene EG11698;galM.
    HOGENOM [Family / Alignment / Tree]
    Family and domain databases
    InterPro IPR008183;Ald1_epimerase.
    IPR011013;Gal_mut_like.
    IPR013458;GalM_Leloir.
    Graphical view of domain structure
    Pfam PF01263;Aldose_epim;1.
    Pfam graphical view of domain structure
    TIGRFAMs TIGR02636;galM_Leloir;1.
    BLOCKS P0A9C3
    PROSITE PS00545;ALDOSE_1_EPIMERASE;1.
    Genome annotation databases
    GenomeReviews U00096_GR;b0756.
    Other
    LinkHub P0A9C3;-.
    ProtoNet P0A9C3
    UniRef View cluster of proteins with at least 50% / 90% / 100% identity
    Keyword
    Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Isomerase;
    Features
    Feature table viewer Feature aligner
    Key  From   To Length  Description  FTId
    CHAIN    1   346    346  Aldose 1-epimerase  PRO_0000197443
    ACT_SITE  175   175    Proton donor(by similarity)  
    ACT_SITE  309   309    Proton acceptor(by similarity)  
    BINDING   79    79    Substrate(by similarity)  
    BINDING  245   245    Substrate(by similarity)  
    Sequence information
    Length: 346AA [This is the length of the unprocessed precursor] Molecular weight: 38190Da [This is the MW of the unprocessed precursor] CRC64: 4373732BAEA83E1D[This is a checksum on the sequence]
            10         20         30         40         50         60
    MLNETPALAP DGQPYRLLTL RNNAGMVVTL MDWGATLLSA RIPLSDGSVR EALLGCASPE
            70         80         90        100        110        120
    CYQDQAAFLG ASIGRYANRI ANSRYTFDGE TVTLSPSQGV NQLHGGPEGF DKRRWQIVNQ
           130        140        150        160        170        180
    NDRQVLFALS SDDGDQGFPG NLGATVQYRL TDDNRISITY RATVDKPCPV NMTNHVYFNL
           190        200        210        220        230        240
    DGEQSDVRNH KLQILADEYL PVDEGGIPHD GLKSVAGTSF DFRSAKIIAS EFLADDDQRK
           250        260        270        280        290        300
    VKGYDHAFLL QAKGDGKKVA AHVWSADEKL QLKVYTTAPA LQFYSGNFLG GTPSRGTEPY
           310        320        330        340 
    ADWQGLALES EFLPDSPNHP EWPQPDCFLR PGEEYSSLTE YQFIAE
    P0A9C3 in FASTA format