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Q96C23 (GALM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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
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
Gene names
Name:GALM
ORF Names:BLOCK25
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 By similarity. Ref.3 Ref.6

Catalytic activity

Alpha-D-glucose = beta-D-glucose.

Pathway

Carbohydrate metabolism; hexose metabolism.

Subunit structure

Monomer.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the aldose epimerase family.

Sequence caution

The sequence AAL62475.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   Molecular functionIsomerase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processhexose metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaldose 1-epimerase activity

Inferred from electronic annotation. Source: EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 342341Aldose 1-epimerase
PRO_0000197433

Regions

Region81 – 822Substrate binding

Sites

Active site1761Proton donor
Active site3071Proton acceptor
Binding site2431Substrate

Amino acid modifications

Modified residue21N-acetylalanine Ref.4

Natural variations

Natural variant1901N → Y.
Corresponds to variant rs6741892 [ dbSNP | Ensembl ].
VAR_024451

Experimental info

Mutagenesis1071H → A: Reduces activity over 5-fold. Ref.3
Mutagenesis1761H → A: Loss of activity. Ref.3
Mutagenesis3071E → A: Loss of activity. Ref.3

Secondary structure

1 ............................................................. 342
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96C23 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 611A54AE7E85813E

FASTA34237,766
        10         20         30         40         50         60 
MASVTRAVFG ELPSGGGTVE KFQLQSDLLR VDIISWGCTI TALEVKDRQG RASDVVLGFA 

        70         80         90        100        110        120 
ELEGYLQKQP YFGAVIGRVA NRIAKGTFKV DGKEYHLAIN KEPNSLHGGV RGFDKVLWTP 

       130        140        150        160        170        180 
RVLSNGVQFS RISPDGEEGY PGELKVWVTY TLDGGELIVN YRAQASQATP VNLTNHSYFN 

       190        200        210        220        230        240 
LAGQASPNIN DHEVTIEADT YLPVDETLIP TGEVAPVQGT AFDLRKPVEL GKHLQDFHLN 

       250        260        270        280        290        300 
GFDHNFCLKG SKEKHFCARV HHAASGRVLE VYTTQPGVQF YTGNFLDGTL KGKNGAVYPK 

       310        320        330        340 
HSGFCLETQN WPDAVNQPRF PPVLLRPGEE YDHTTWFKFS VA

« Hide

References

« Hide 'large scale' references
[1]"Physical/genetic map of the 2p22-2p21 region on chromosome 2."
Gorry M.C., Zhang Y., Marks J.J., Suppes B., Hart P.S., Cortelli J.R., Pallos D., Hart T.C.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Skin.
[3]"Identification and characterisation of human aldose 1-epimerase."
Timson D.J., Reece R.J.
FEBS Lett. 543:21-24(2003) [PubMed: 12753898] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF HIS-107; HIS-176 AND GLU-307.
[4]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Molecular structure of human galactose mutarotase."
Thoden J.B., Timson D.J., Reece R.J., Holden H.M.
J. Biol. Chem. 279:23431-23437(2004) [PubMed: 15026423] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY064382 expand/collapse EMBL AC list , AY064381, AY064379, AY064380, AY064378 Genomic DNA. Translation: AAL62475.1. Sequence problems.
AY064385 expand/collapse EMBL AC list , AY064378, AY064380, AY064379, AY064381, AY064384, AY064383 Genomic DNA. Translation: AAL62476.1.
BC014916 mRNA. Translation: AAH14916.1.
BC019263 mRNA. Translation: AAH19263.1.
IPIIPI00060200.
RefSeqNP_620156.1. NM_138801.2.
UniGeneHs.435012.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SNZX-ray2.20A/B1-342[»]
1SO0X-ray2.30A/B/C/D1-342[»]
ProteinModelPortalQ96C23.
SMRQ96C23. Positions 1-342.
ModBaseSearch...

Protein-protein interaction databases

IntActQ96C23. 1 interaction.
STRINGQ96C23.

Polymorphism databases

DMDM67463772.

Proteomic databases

PeptideAtlasQ96C23.
PRIDEQ96C23.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272252; ENSP00000272252; ENSG00000143891.
GeneID130589.
KEGGhsa:130589.
UCSCuc002rqy.1. human.

Organism-specific databases

CTD130589.
GeneCardsGC02P038867.
H-InvDBHIX0001987.
HGNCHGNC:24063. GALM.
HPAHPA035472.
MIM608883. gene.
neXtProtNX_Q96C23.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00510000047589.
HOGENOMHBG703640.
HOVERGENHBG051697.
InParanoidQ96C23.
OMAMVSVTRA.
OrthoDBEOG4HHP31.
PhylomeDBQ96C23.

Enzyme and pathway databases

BioCycMetaCyc:HS07125-MONOMER.

Gene expression databases

ArrayExpressQ96C23.
BgeeQ96C23.
CleanExHS_GALM.
GenevestigatorQ96C23.
GermOnlineENSG00000143891. Homo sapiens.

Family and domain databases

InterProIPR018052. Ald1_epimerase_CS.
IPR008183. Aldose_1-epimerase.
IPR015443. Aldose_1-epimerase_subgr.
IPR011013. Glyco_hydro-type_carb-bd.
IPR014718. Glyco_hydro-type_carb-bd_sub.
[Graphical view]
Gene3DG3DSA:2.70.98.10. Glyco_hydro_42_D5. 1 hit.
KOK01785.
PANTHERPTHR10091. Ald_epimerase. 1 hit.
PfamPF01263. Aldose_epim. 1 hit.
[Graphical view]
SUPFAMSSF74650. Gal_mut_like. 1 hit.
PROSITEPS00545. ALDOSE_1_EPIMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio82783.
SOURCESearch...

Entry information

Entry nameGALM_HUMAN
AccessionPrimary (citable) accession number: Q96C23
Secondary accession number(s): Q8NIA2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents