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Protein

Bifunctional protein GAL10

Gene

GAL10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

UDP-alpha-D-glucose = UDP-alpha-D-galactose.
Alpha-D-glucose = beta-D-glucose.PROSITE-ProRule annotation

Cofactori

Pathwayi: galactose metabolism

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

Pathwayi: hexose metabolism

This protein is involved in the pathway hexose metabolism, which is part of Carbohydrate metabolism.
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)DescriptionActionsGraphical viewLength
Active sitei537For mutarotase activitySequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 44NADSequence analysisAdd BLAST32

GO - Molecular functioni

  • aldose 1-epimerase activity Source: SGD
  • carbohydrate binding Source: InterPro
  • UDP-glucose 4-epimerase activity Source: SGD

GO - Biological processi

  • galactose catabolic process via UDP-galactose Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Galactose metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciYEAST:YBR019C-MONOMER.
ReactomeiR-SCE-70370. Galactose catabolism.
UniPathwayiUPA00214.
UPA00242.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein GAL10
Including the following 2 domains:
UDP-glucose 4-epimerase (EC:5.1.3.2)
Alternative name(s):
Galactowaldenase
Aldose 1-epimerase (EC:5.1.3.3)
Alternative name(s):
Galactose mutarotase
Gene namesi
Name:GAL10
Ordered Locus Names:YBR019C
ORF Names:YBR0301
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR019C.
SGDiS000000223. GAL10.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001974421 – 699Bifunctional protein GAL10Add BLAST699

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei562PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP04397.
TopDownProteomicsiP04397.

PTM databases

iPTMnetiP04397.

Expressioni

Inductioni

By galactose.

Interactioni

Protein-protein interaction databases

BioGridi32722. 56 interactors.
DIPiDIP-4891N.
MINTiMINT-526001.

Structurei

Secondary structure

1699
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 17Combined sources5
Turni18 – 20Combined sources3
Helixi22 – 33Combined sources12
Beta strandi37 – 42Combined sources6
Helixi50 – 59Combined sources10
Beta strandi65 – 67Combined sources3
Helixi73 – 82Combined sources10
Beta strandi87 – 90Combined sources4
Helixi97 – 102Combined sources6
Helixi104 – 125Combined sources22
Beta strandi129 – 135Combined sources7
Helixi136 – 139Combined sources4
Helixi142 – 144Combined sources3
Helixi162 – 180Combined sources19
Beta strandi186 – 192Combined sources7
Beta strandi194 – 196Combined sources3
Beta strandi209 – 211Combined sources3
Helixi215 – 223Combined sources9
Beta strandi226 – 228Combined sources3
Beta strandi248 – 250Combined sources3
Helixi251 – 267Combined sources17
Beta strandi274 – 281Combined sources8
Helixi288 – 299Combined sources12
Helixi323 – 328Combined sources6
Helixi337 – 350Combined sources14
Beta strandi360 – 367Combined sources8
Beta strandi373 – 379Combined sources7
Beta strandi382 – 391Combined sources10
Beta strandi395 – 400Combined sources6
Helixi412 – 415Combined sources4
Beta strandi432 – 434Combined sources3
Helixi435 – 437Combined sources3
Beta strandi438 – 441Combined sources4
Beta strandi444 – 447Combined sources4
Beta strandi455 – 457Combined sources3
Helixi460 – 462Combined sources3
Helixi464 – 466Combined sources3
Beta strandi470 – 478Combined sources9
Beta strandi481 – 490Combined sources10
Helixi492 – 494Combined sources3
Beta strandi495 – 510Combined sources16
Turni511 – 514Combined sources4
Beta strandi515 – 531Combined sources17
Turni542 – 545Combined sources4
Beta strandi548 – 550Combined sources3
Beta strandi553 – 558Combined sources6
Beta strandi561 – 565Combined sources5
Beta strandi571 – 577Combined sources7
Beta strandi585 – 587Combined sources3
Beta strandi589 – 591Combined sources3
Beta strandi599 – 604Combined sources6
Beta strandi621 – 627Combined sources7
Turni629 – 631Combined sources3
Beta strandi634 – 647Combined sources14
Beta strandi662 – 668Combined sources7
Helixi672 – 674Combined sources3
Turni676 – 678Combined sources3
Helixi679 – 682Combined sources4
Beta strandi683 – 685Combined sources3
Beta strandi689 – 699Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z45X-ray1.85A1-699[»]
ProteinModelPortaliP04397.
SMRiP04397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04397.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 357GalactowaldenaseAdd BLAST357
Regioni358 – 699MutarotaseAdd BLAST342

Sequence similaritiesi

In the N-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family.Curated
In the C-terminal section; belongs to the aldose epimerase family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000063128.
HOGENOMiHOG000247896.
InParanoidiP04397.
KOiK01784.
K01785.
OMAiDLWKWTT.
OrthoDBiEOG092C4CZ3.

Family and domain databases

Gene3Di2.70.98.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR018052. Ald1_epimerase_CS.
IPR008183. Aldose_1/G6P_1-epimerase.
IPR011013. Gal_mutarotase_SF_dom.
IPR005886. GalE.
IPR014718. GH-type_carb-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01263. Aldose_epim. 1 hit.
PF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF74650. SSF74650. 1 hit.
TIGRFAMsiTIGR01179. galE. 1 hit.
PROSITEiPS00545. ALDOSE_1_EPIMERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04397-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAQLQSEST SKIVLVTGGA GYIGSHTVVE LIENGYDCVV ADNLSNSTYD
60 70 80 90 100
SVARLEVLTK HHIPFYEVDL CDRKGLEKVF KEYKIDSVIH FAGLKAVGES
110 120 130 140 150
TQIPLRYYHN NILGTVVLLE LMQQYNVSKF VFSSSATVYG DATRFPNMIP
160 170 180 190 200
IPEECPLGPT NPYGHTKYAI ENILNDLYNS DKKSWKFAIL RYFNPIGAHP
210 220 230 240 250
SGLIGEDPLG IPNNLLPYMA QVAVGRREKL YIFGDDYDSR DGTPIRDYIH
260 270 280 290 300
VVDLAKGHIA ALQYLEAYNE NEGLCREWNL GSGKGSTVFE VYHAFCKASG
310 320 330 340 350
IDLPYKVTGR RAGDVLNLTA KPDRAKRELK WQTELQVEDS CKDLWKWTTE
360 370 380 390 400
NPFGYQLRGV EARFSAEDMR YDARFVTIGA GTRFQATFAN LGASIVDLKV
410 420 430 440 450
NGQSVVLGYE NEEGYLNPDS AYIGATIGRY ANRISKGKFS LCNKDYQLTV
460 470 480 490 500
NNGVNANHSS IGSFHRKRFL GPIIQNPSKD VFTAEYMLID NEKDTEFPGD
510 520 530 540 550
LLVTIQYTVN VAQKSLEMVY KGKLTAGEAT PINLTNHSYF NLNKPYGDTI
560 570 580 590 600
EGTEIMVRSK KSVDVDKNMI PTGNIVDREI ATFNSTKPTV LGPKNPQFDC
610 620 630 640 650
CFVVDENAKP SQINTLNNEL TLIVKAFHPD SNITLEVLST EPTYQFYTGD
660 670 680 690
FLSAGYEARQ GFAIEPGRYI DAINQENWKD CVTLKNGETY GSKIVYRFS
Length:699
Mass (Da):78,195
Last modified:October 1, 1994 - v2
Checksum:i8354BAFF65D06934
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti302 – 306DLPYK → WSSVR no nucleotide entry (PubMed:6715281).Curated5
Sequence conflicti464F → L no nucleotide entry (PubMed:6715281).Curated1
Sequence conflicti479 – 480KD → NY no nucleotide entry (PubMed:6715281).Curated2
Sequence conflicti498P → Q no nucleotide entry (PubMed:6715281).Curated1
Sequence conflicti518M → I no nucleotide entry (PubMed:6715281).Curated1
Sequence conflicti667G → C no nucleotide entry (PubMed:6715281).Curated1
Sequence conflicti694 – 695IV → TL no nucleotide entry (PubMed:6715281).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35888 Genomic DNA. Translation: CAA84961.1.
X81324 Genomic DNA. Translation: CAA57106.1.
K02115 Genomic DNA. Translation: AAA34620.1.
M12348 Genomic DNA. No translation available.
K01609 Genomic DNA. Translation: AAA34630.1.
BK006936 Genomic DNA. Translation: DAA07141.1.
PIRiS45875. XEBYUG.
RefSeqiNP_009575.1. NM_001178367.1.

Genome annotation databases

EnsemblFungiiYBR019C; YBR019C; YBR019C.
GeneIDi852307.
KEGGisce:YBR019C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35888 Genomic DNA. Translation: CAA84961.1.
X81324 Genomic DNA. Translation: CAA57106.1.
K02115 Genomic DNA. Translation: AAA34620.1.
M12348 Genomic DNA. No translation available.
K01609 Genomic DNA. Translation: AAA34630.1.
BK006936 Genomic DNA. Translation: DAA07141.1.
PIRiS45875. XEBYUG.
RefSeqiNP_009575.1. NM_001178367.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z45X-ray1.85A1-699[»]
ProteinModelPortaliP04397.
SMRiP04397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32722. 56 interactors.
DIPiDIP-4891N.
MINTiMINT-526001.

PTM databases

iPTMnetiP04397.

Proteomic databases

PRIDEiP04397.
TopDownProteomicsiP04397.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR019C; YBR019C; YBR019C.
GeneIDi852307.
KEGGisce:YBR019C.

Organism-specific databases

EuPathDBiFungiDB:YBR019C.
SGDiS000000223. GAL10.

Phylogenomic databases

GeneTreeiENSGT00530000063128.
HOGENOMiHOG000247896.
InParanoidiP04397.
KOiK01784.
K01785.
OMAiDLWKWTT.
OrthoDBiEOG092C4CZ3.

Enzyme and pathway databases

UniPathwayiUPA00214.
UPA00242.
BioCyciYEAST:YBR019C-MONOMER.
ReactomeiR-SCE-70370. Galactose catabolism.

Miscellaneous databases

EvolutionaryTraceiP04397.
PROiP04397.

Family and domain databases

Gene3Di2.70.98.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR018052. Ald1_epimerase_CS.
IPR008183. Aldose_1/G6P_1-epimerase.
IPR011013. Gal_mutarotase_SF_dom.
IPR005886. GalE.
IPR014718. GH-type_carb-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01263. Aldose_epim. 1 hit.
PF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF74650. SSF74650. 1 hit.
TIGRFAMsiTIGR01179. galE. 1 hit.
PROSITEiPS00545. ALDOSE_1_EPIMERASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGAL10_YEAST
AccessioniPrimary (citable) accession number: P04397
Secondary accession number(s): D6VQ21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: October 1, 1994
Last modified: November 2, 2016
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

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.