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Protein

Aldose 1-epimerase

Gene

GALM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

Alpha-D-glucose = beta-D-glucose.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei176 – 1761Proton donor
Binding sitei243 – 2431Substrate1 Publication
Active sitei307 – 3071Proton acceptor

GO - Molecular functioni

  1. aldose 1-epimerase activity Source: UniProtKB
  2. carbohydrate binding Source: InterPro

GO - Biological processi

  1. galactose metabolic process Source: UniProtKB
  2. glucose metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS07125-MONOMER.
BRENDAi5.1.3.3. 2681.
SABIO-RKQ96C23.
SignaLinkiQ96C23.
UniPathwayiUPA00242.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldose 1-epimerase (EC:5.1.3.3)
Alternative name(s):
Galactose mutarotase
Gene namesi
Name:GALM
ORF Names:BLOCK25
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:24063. GALM.

Subcellular locationi

  1. Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071H → A: Reduces activity over 5-fold. 1 Publication
Mutagenesisi176 – 1761H → A: Loss of activity. 1 Publication
Mutagenesisi307 – 3071E → A: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA134980075.

Polymorphism and mutation databases

BioMutaiGALM.
DMDMi67463772.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 342341Aldose 1-epimerasePRO_0000197433Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ96C23.
PaxDbiQ96C23.
PeptideAtlasiQ96C23.
PRIDEiQ96C23.

PTM databases

PhosphoSiteiQ96C23.

Expressioni

Gene expression databases

BgeeiQ96C23.
CleanExiHS_GALM.
ExpressionAtlasiQ96C23. baseline and differential.
GenevestigatoriQ96C23.

Organism-specific databases

HPAiHPA035472.
HPA035473.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi126244. 1 interaction.
IntActiQ96C23. 1 interaction.
MINTiMINT-5001489.
STRINGi9606.ENSP00000272252.

Structurei

Secondary structure

1
342
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1210Combined sources
Turni13 – 164Combined sources
Beta strandi17 – 259Combined sources
Beta strandi30 – 345Combined sources
Beta strandi39 – 468Combined sources
Beta strandi52 – 543Combined sources
Helixi62 – 665Combined sources
Beta strandi81 – 833Combined sources
Helixi84 – 863Combined sources
Beta strandi87 – 904Combined sources
Beta strandi93 – 964Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi109 – 1113Combined sources
Helixi113 – 1153Combined sources
Beta strandi119 – 1235Combined sources
Beta strandi126 – 1338Combined sources
Helixi137 – 1393Combined sources
Beta strandi144 – 15310Combined sources
Beta strandi156 – 16712Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi198 – 2014Combined sources
Helixi230 – 2367Combined sources
Beta strandi243 – 2486Combined sources
Beta strandi251 – 2533Combined sources
Beta strandi255 – 2617Combined sources
Turni263 – 2653Combined sources
Beta strandi267 – 28115Combined sources
Beta strandi287 – 2915Combined sources
Helixi293 – 2953Combined sources
Beta strandi297 – 2993Combined sources
Beta strandi304 – 3107Combined sources
Helixi314 – 3163Combined sources
Beta strandi331 – 34111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SNZX-ray2.20A/B1-342[»]
1SO0X-ray2.30A/B/C/D1-342[»]
ProteinModelPortaliQ96C23.
SMRiQ96C23. Positions 1-342.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96C23.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 822Substrate binding

Sequence similaritiesi

Belongs to the aldose epimerase family.Curated

Phylogenomic databases

eggNOGiCOG2017.
GeneTreeiENSGT00510000047589.
HOGENOMiHOG000072798.
HOVERGENiHBG051697.
InParanoidiQ96C23.
KOiK01785.
OMAiDADCVAE.
OrthoDBiEOG7V7666.
PhylomeDBiQ96C23.
TreeFamiTF324207.

Family and domain databases

Gene3Di2.70.98.10. 1 hit.
InterProiIPR018052. Ald1_epimerase_CS.
IPR015443. Aldose_1-epimerase.
IPR008183. Aldose_1/G6P_1-epimerase.
IPR011013. Gal_mutarotase_SF_dom.
IPR014718. Glyco_hydro-type_carb-bd_sub.
[Graphical view]
PfamiPF01263. Aldose_epim. 1 hit.
[Graphical view]
PIRSFiPIRSF005096. GALM. 1 hit.
SUPFAMiSSF74650. SSF74650. 1 hit.
PROSITEiPS00545. ALDOSE_1_EPIMERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96C23-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVTRAVFG ELPSGGGTVE KFQLQSDLLR VDIISWGCTI TALEVKDRQG
60 70 80 90 100
RASDVVLGFA ELEGYLQKQP YFGAVIGRVA NRIAKGTFKV DGKEYHLAIN
110 120 130 140 150
KEPNSLHGGV RGFDKVLWTP RVLSNGVQFS RISPDGEEGY PGELKVWVTY
160 170 180 190 200
TLDGGELIVN YRAQASQATP VNLTNHSYFN LAGQASPNIN DHEVTIEADT
210 220 230 240 250
YLPVDETLIP TGEVAPVQGT AFDLRKPVEL GKHLQDFHLN GFDHNFCLKG
260 270 280 290 300
SKEKHFCARV HHAASGRVLE VYTTQPGVQF YTGNFLDGTL KGKNGAVYPK
310 320 330 340
HSGFCLETQN WPDAVNQPRF PPVLLRPGEE YDHTTWFKFS VA
Length:342
Mass (Da):37,766
Last modified:December 1, 2001 - v1
Checksum:i611A54AE7E85813E
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti190 – 1901N → Y.
Corresponds to variant rs6741892 [ dbSNP | Ensembl ].
VAR_024451

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY064382
, AY064381, AY064379, AY064380, AY064378 Genomic DNA. Translation: AAL62475.1. Sequence problems.
AY064385
, AY064378, AY064380, AY064379, AY064381, AY064384, AY064383 Genomic DNA. Translation: AAL62476.1.
EU794611 mRNA. Translation: ACJ13665.1.
AK291489 mRNA. Translation: BAF84178.1.
AC074366 Genomic DNA. Translation: AAX93101.1.
CH471053 Genomic DNA. Translation: EAX00367.1.
BC014916 mRNA. Translation: AAH14916.1.
BC019263 mRNA. Translation: AAH19263.1.
CCDSiCCDS1797.1.
RefSeqiNP_620156.1. NM_138801.2.
UniGeneiHs.435012.

Genome annotation databases

EnsembliENST00000272252; ENSP00000272252; ENSG00000143891.
GeneIDi130589.
KEGGihsa:130589.
UCSCiuc002rqy.3. human.

Polymorphism and mutation databases

BioMutaiGALM.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY064382
, AY064381, AY064379, AY064380, AY064378 Genomic DNA. Translation: AAL62475.1. Sequence problems.
AY064385
, AY064378, AY064380, AY064379, AY064381, AY064384, AY064383 Genomic DNA. Translation: AAL62476.1.
EU794611 mRNA. Translation: ACJ13665.1.
AK291489 mRNA. Translation: BAF84178.1.
AC074366 Genomic DNA. Translation: AAX93101.1.
CH471053 Genomic DNA. Translation: EAX00367.1.
BC014916 mRNA. Translation: AAH14916.1.
BC019263 mRNA. Translation: AAH19263.1.
CCDSiCCDS1797.1.
RefSeqiNP_620156.1. NM_138801.2.
UniGeneiHs.435012.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SNZX-ray2.20A/B1-342[»]
1SO0X-ray2.30A/B/C/D1-342[»]
ProteinModelPortaliQ96C23.
SMRiQ96C23. Positions 1-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126244. 1 interaction.
IntActiQ96C23. 1 interaction.
MINTiMINT-5001489.
STRINGi9606.ENSP00000272252.

PTM databases

PhosphoSiteiQ96C23.

Polymorphism and mutation databases

BioMutaiGALM.
DMDMi67463772.

Proteomic databases

MaxQBiQ96C23.
PaxDbiQ96C23.
PeptideAtlasiQ96C23.
PRIDEiQ96C23.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272252; ENSP00000272252; ENSG00000143891.
GeneIDi130589.
KEGGihsa:130589.
UCSCiuc002rqy.3. human.

Organism-specific databases

CTDi130589.
GeneCardsiGC02P038867.
HGNCiHGNC:24063. GALM.
HPAiHPA035472.
HPA035473.
MIMi137030. gene.
neXtProtiNX_Q96C23.
PharmGKBiPA134980075.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2017.
GeneTreeiENSGT00510000047589.
HOGENOMiHOG000072798.
HOVERGENiHBG051697.
InParanoidiQ96C23.
KOiK01785.
OMAiDADCVAE.
OrthoDBiEOG7V7666.
PhylomeDBiQ96C23.
TreeFamiTF324207.

Enzyme and pathway databases

UniPathwayiUPA00242.
BioCyciMetaCyc:HS07125-MONOMER.
BRENDAi5.1.3.3. 2681.
SABIO-RKQ96C23.
SignaLinkiQ96C23.

Miscellaneous databases

ChiTaRSiGALM. human.
EvolutionaryTraceiQ96C23.
GeneWikiiGalactose_mutarotase.
GenomeRNAii130589.
NextBioi82783.
PROiQ96C23.
SOURCEiSearch...

Gene expression databases

BgeeiQ96C23.
CleanExiHS_GALM.
ExpressionAtlasiQ96C23. baseline and differential.
GenevestigatoriQ96C23.

Family and domain databases

Gene3Di2.70.98.10. 1 hit.
InterProiIPR018052. Ald1_epimerase_CS.
IPR015443. Aldose_1-epimerase.
IPR008183. Aldose_1/G6P_1-epimerase.
IPR011013. Gal_mutarotase_SF_dom.
IPR014718. Glyco_hydro-type_carb-bd_sub.
[Graphical view]
PfamiPF01263. Aldose_epim. 1 hit.
[Graphical view]
PIRSFiPIRSF005096. GALM. 1 hit.
SUPFAMiSSF74650. SSF74650. 1 hit.
PROSITEiPS00545. ALDOSE_1_EPIMERASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Li J.Y., Wang H.Y., Liu F.J., Liu J.
    Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Skin.
  7. "Identification and characterisation of human aldose 1-epimerase."
    Timson D.J., Reece R.J.
    FEBS Lett. 543:21-24(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF HIS-107; HIS-176 AND GLU-307.
  8. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION.

Entry informationi

Entry nameiGALM_HUMAN
AccessioniPrimary (citable) accession number: Q96C23
Secondary accession number(s): Q53RY1, Q8NIA2, V9HWA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: December 1, 2001
Last modified: April 29, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.