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P0A9C3 (GALM_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldose 1-epimerase

EC=5.1.3.3
Alternative name(s):
Galactose mutarotase
Type-1 mutarotase
Gene names
Name:galM
Ordered Locus Names:b0756, JW0739
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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

Carbohydrate metabolism; hexose metabolism.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the aldose epimerase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processgalactose catabolic process via UDP-galactose

Inferred from mutant phenotype Ref.1. Source: EcoCyc

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 5337146. Source: EcoCyc

   Molecular_functionaldose 1-epimerase activity

Inferred from direct assay PubMed 4945113. Source: EcoCyc

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346Aldose 1-epimerase
PRO_0000197443

Sites

Active site1751Proton donor By similarity
Active site3091Proton acceptor By similarity
Binding site791Substrate By similarity
Binding site2451Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A9C3 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 4373732BAEA83E1D

FASTA34638,190
        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 

« Hide

References

« Hide 'large scale' references
[1]"Dependence of lactose metabolism upon mutarotase encoded in the gal operon in Escherichia coli."
Bouffard G.G., Rudd K.E., Adhya S.L.
J. Mol. Biol. 244:269-278(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14.
Strain: K12 / SA1308.
[2]"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."
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. expand/collapse author list , 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.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U13636 Genomic DNA. Translation: AAB17020.1.
U00096 Genomic DNA. Translation: AAC73843.1.
AP009048 Genomic DNA. Translation: BAA35418.1.
PIRD64811.
RefSeqNP_415277.1. NC_000913.2.
YP_489029.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0A9C3.
SMRP0A9C3. Positions 28-343.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-35901N.
IntActP0A9C3. 4 interactions.
MINTMINT-1249454.
STRING511145.b0756.

2D gel databases

SWISS-2DPAGEP0A9C3.

Proteomic databases

PaxDbP0A9C3.
PRIDEP0A9C3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73843; AAC73843; b0756.
BAA35418; BAA35418; BAA35418.
GeneID12932716.
944943.
KEGGecj:Y75_p0729.
eco:b0756.
PATRIC32116713. VBIEscCol129921_0782.

Organism-specific databases

EchoBASEEB1649.
EcoGeneEG11698. galM.

Phylogenomic databases

eggNOGCOG2017.
HOGENOMHOG000072798.
KOK01785.
OMAQLHSPDG.
ProtClustDBPRK11055.

Enzyme and pathway databases

BioCycEcoCyc:ALDOSE1EPIM-MONOMER.
ECOL316407:JW0739-MONOMER.
MetaCyc:ALDOSE1EPIM-MONOMER.
SABIO-RKP0A9C3.
UniPathwayUPA00242.

Gene expression databases

GenevestigatorP0A9C3.

Family and domain databases

Gene3D2.70.98.10. 1 hit.
InterProIPR018052. Ald1_epimerase_CS.
IPR013458. Ald_epimerase_bac.
IPR015443. Aldose_1-epimerase.
IPR008183. Aldose_1/G6P_1-epimerase.
IPR011013. Gal_mutarotase_SF_dom.
IPR014718. Glyco_hydro-type_carb-bd_sub.
[Graphical view]
PANTHERPTHR10091. PTHR10091. 1 hit.
PfamPF01263. Aldose_epim. 1 hit.
[Graphical view]
PIRSFPIRSF005096. GALM. 1 hit.
SUPFAMSSF74650. Gal_mut_like. 1 hit.
TIGRFAMsTIGR02636. galM_Leloir. 1 hit.
PROSITEPS00545. ALDOSE_1_EPIMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGALM_ECOLI
AccessionPrimary (citable) accession number: P0A9C3
Secondary accession number(s): P40681
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families