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Protein

Aldose 1-epimerase

Gene

galM

Organism
Lactococcus lactis
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Converts alpha-aldose to the beta-anomer.UniRule annotation

Catalytic activityi

Alpha-D-glucose = beta-D-glucose.UniRule annotation

Pathwayi: hexose metabolism

This protein is involved in the pathway hexose metabolism, which is part of Carbohydrate metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway hexose metabolism and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei71 – 711FucoseCombined sources
Binding sitei71 – 711GalactoseCombined sources
Binding sitei71 – 711GlucoseCombined sources
Binding sitei96 – 961FucoseCombined sources
Binding sitei96 – 961GalactoseCombined sources
Binding sitei96 – 961GlucoseCombined sources
Active sitei170 – 1701Proton donorUniRule annotation
Binding sitei170 – 1701FucoseCombined sources
Binding sitei172 – 1721GlucoseCombined sources
Binding sitei203 – 2031FucoseCombined sources
Binding sitei203 – 2031GalactoseCombined sources
Binding sitei203 – 2031GlucoseCombined sources
Binding sitei243 – 2431FucoseCombined sources
Binding sitei243 – 2431GalactoseCombined sources
Binding sitei243 – 2431GlucoseCombined sources
Binding sitei243 – 2431SubstrateUniRule annotation
Binding sitei279 – 2791FucoseCombined sources
Binding sitei279 – 2791GalactoseCombined sources
Binding sitei279 – 2791GlucoseCombined sources
Active sitei304 – 3041Proton acceptorUniRule annotation
Binding sitei304 – 3041FucoseCombined sources
Binding sitei304 – 3041GalactoseCombined sources
Binding sitei304 – 3041GlucoseCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

IsomeraseUniRule annotation

Keywords - Biological processi

Carbohydrate metabolismUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00242.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldose 1-epimeraseUniRule annotation (EC:5.1.3.3UniRule annotation)
Alternative name(s):
Galactose mutarotaseUniRule annotation
Gene namesi
Name:galMImported
OrganismiLactococcus lactisImported
Taxonomic identifieri1358 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

PTM / Processingi

Proteomic databases

PaxDbiQ9ZB17.

Interactioni

Protein-protein interaction databases

STRINGi272623.L0029.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L7JX-ray1.90A/B1-339[»]
1L7KX-ray1.95A/B1-339[»]
1MMUX-ray1.80A/B1-339[»]
1MMXX-ray1.80A/B1-339[»]
1MMYX-ray1.85A/B1-339[»]
1MMZX-ray1.80A/B1-339[»]
1MN0X-ray1.90A/B1-339[»]
1NS0X-ray1.85A/B3-339[»]
1NS2X-ray1.95A/B3-339[»]
1NS4X-ray1.85A/B3-339[»]
1NS7X-ray1.85A/B3-339[»]
1NS8X-ray1.80A/B3-339[»]
1NSMX-ray1.85A/B3-339[»]
1NSRX-ray1.80A/B3-339[»]
1NSSX-ray1.85A/B3-339[»]
1NSUX-ray1.80A/B3-339[»]
1NSVX-ray1.80A/B3-339[»]
1NSXX-ray1.75A/B3-339[»]
1NSZX-ray1.75A/B3-339[»]
ProteinModelPortaliQ9ZB17.
SMRiQ9ZB17. Positions 3-339.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZB17.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni170 – 1723Galactose bindingCombined sources

Sequence similaritiesi

Belongs to the aldose epimerase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105ENN. Bacteria.
COG2017. LUCA.

Family and domain databases

Gene3Di2.70.98.10. 1 hit.
InterProiIPR013458. Ald_epimerase_bac.
IPR015443. Aldose_1-epimerase.
IPR008183. Aldose_1/G6P_1-epimerase.
IPR011013. Gal_mutarotase_SF_dom.
IPR014718. GH-type_carb-bd.
[Graphical view]
PfamiPF01263. Aldose_epim. 1 hit.
[Graphical view]
PIRSFiPIRSF005096. GALM. 1 hit.
SUPFAMiSSF74650. SSF74650. 1 hit.
TIGRFAMsiTIGR02636. galM_Leloir. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9ZB17-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIKIRDFGL GSDLISLTNK AGVTISFTNL GARIVDWQKD GKHLILGFDS
60 70 80 90 100
AKEYLEKDAY PGATVGPTAG RIKDGLVKIS GKDYILNQNE GPQTLHGGEE
110 120 130 140 150
SIHTKLWTYE VTDLGAEVQV KFSLVTNDGT NGYPGKIEMS VTHSFDDYNK
160 170 180 190 200
WKIHYEAISD KDTVFNPTGH VYFNLNGDAS ESVENHGLRL AASRFVPLKD
210 220 230 240 250
QTEIVRGDIV DIKNTDLDFR QEKQLSNAFN SNMEQVQLVK GIDHPFLLDQ
260 270 280 290 300
LGLDKEQARL TLDDTSISVF TDQPSIVIFT ANFGDLGTLY HEKKQVHHGG
310 320 330
ITFECQVSPG SEQIPELGDI SLKAGEKYQA TTIYSLHTK
Length:339
Mass (Da):37,611
Last modified:May 1, 1999 - v1
Checksum:i65053E6517D1DF2C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60828 Genomic DNA. Translation: AAD11509.1.
RefSeqiWP_039116219.1. NZ_LDEK01000003.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60828 Genomic DNA. Translation: AAD11509.1.
RefSeqiWP_039116219.1. NZ_LDEK01000003.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L7JX-ray1.90A/B1-339[»]
1L7KX-ray1.95A/B1-339[»]
1MMUX-ray1.80A/B1-339[»]
1MMXX-ray1.80A/B1-339[»]
1MMYX-ray1.85A/B1-339[»]
1MMZX-ray1.80A/B1-339[»]
1MN0X-ray1.90A/B1-339[»]
1NS0X-ray1.85A/B3-339[»]
1NS2X-ray1.95A/B3-339[»]
1NS4X-ray1.85A/B3-339[»]
1NS7X-ray1.85A/B3-339[»]
1NS8X-ray1.80A/B3-339[»]
1NSMX-ray1.85A/B3-339[»]
1NSRX-ray1.80A/B3-339[»]
1NSSX-ray1.85A/B3-339[»]
1NSUX-ray1.80A/B3-339[»]
1NSVX-ray1.80A/B3-339[»]
1NSXX-ray1.75A/B3-339[»]
1NSZX-ray1.75A/B3-339[»]
ProteinModelPortaliQ9ZB17.
SMRiQ9ZB17. Positions 3-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272623.L0029.

Proteomic databases

PaxDbiQ9ZB17.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105ENN. Bacteria.
COG2017. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00242.

Miscellaneous databases

EvolutionaryTraceiQ9ZB17.

Family and domain databases

Gene3Di2.70.98.10. 1 hit.
InterProiIPR013458. Ald_epimerase_bac.
IPR015443. Aldose_1-epimerase.
IPR008183. Aldose_1/G6P_1-epimerase.
IPR011013. Gal_mutarotase_SF_dom.
IPR014718. GH-type_carb-bd.
[Graphical view]
PfamiPF01263. Aldose_epim. 1 hit.
[Graphical view]
PIRSFiPIRSF005096. GALM. 1 hit.
SUPFAMiSSF74650. SSF74650. 1 hit.
TIGRFAMsiTIGR02636. galM_Leloir. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and nucleotide sequence of the beta-galactosidase gene from Lactococcus lactis ssp. lactis ATCC7962."
    Lee J.M., Chung D.K., Park J.H., Lee W.K., Chang H.C., Kim J.H., Lee H.J.
    Biotechnol. Lett. 19:179-183(1997)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC7962Imported.
  2. "The organization of genes involved in metabolism of gal/lac of Lactococcus lactis."
    Lee J.M., Chung D.K., Park J.H., Lee W.K., Chang H.C., Kim J.H., Lee H.J.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC7962Imported.
  3. "High resolution X-ray structure of galactose mutarotase from Lactococcus lactis."
    Thoden J.B., Holden H.M.
    J. Biol. Chem. 277:20854-20861(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
  4. "Structural and kinetic studies of sugar binding to galactose mutarotase from Lactococcus lactis."
    Thoden J.B., Kim J., Raushel F.M., Holden H.M.
    J. Biol. Chem. 277:45458-45465(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH FUCOSE.
  5. "The catalytic mechanism of galactose mutarotase."
    Thoden J.B., Kim J., Raushel F.M., Holden H.M.
    Protein Sci. 12:1051-1059(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3-339 IN COMPLEX WITH GALACTOSE AND GLUCOSE.

Entry informationi

Entry nameiQ9ZB17_9LACT
AccessioniPrimary (citable) accession number: Q9ZB17
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: July 6, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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 one 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.