P13045 (GAL3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein GAL3

Gene names

Name:	GAL3
Ordered Locus Names:	YDR009W
ORF Names:	YD8119.14

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The GAL3 regulatory function is required for rapid induction of the galactose system. At normal induction, galactose in the presence of the GAL3 protein may lead to the induction of the GAL genes, including GAL1. Then the galactokinase protein (GAL1) in the presence of galactose may reinforce the induction leading to a higher expression level. Upon depletion of galactose, the inducing activity of the galactokinase protein may decrease, after which transcription of the GAL genes, including GAL1, may decrease.
Induction	The GAL3 gene is a member of the family of galactose inducible, glucose-repressible genes (which include GAL1, GAL2, GAL7, GAL10, GAL80, and MELI).
Miscellaneous	Present with 721 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the GHMP kinase family. GalK subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Galactose metabolism
Ligand	ATP-binding Nucleotide-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	galactose metabolic process Inferred from mutant phenotype PubMed 4577139. Source: SGD maintenance of protein location Inferred from mutant phenotype PubMed 19651897. Source: SGD positive regulation of transcription from RNA polymerase II promoter by galactose Inferred from mutant phenotype PubMed 3013721. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 10866670PubMed 18952899. Source: SGD nucleus Inferred from direct assay PubMed 18952899. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW galactokinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
URE2	P23202	1	EBI-7282,EBI-20138

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 520

520

Protein GAL3

PRO_0000184658

Experimental info

Sequence conflict

37 – 45

9

KPDFIARSP → NLILSLGLL in AAA34625. Ref.1

Sequence conflict

170 – 171

2

AA → GR in AAA34625. Ref.1

Sequence conflict

192 – 211

20

RITAV…GMDQA → ASQRLRSTMLESIMVVWIKQ in AAA34625. Ref.1

Sequence conflict

227 – 241

15

RPKLK…FPQLK → MAKTKWPHFQVSSIE in AAA34625. Ref.1

Sequence conflict

251 – 294

44

NTLVK…SHKDN → ILCTRSNNRTLLHISLSCSL LTLLYISTFAREPCGPDTLG LTISQGQ in AAA34625. Ref.1

Sequence conflict

303 – 338

36

RDFMD…MLQLV → EIYGCLLRPDTKTKPNHGME ISELVLNVYSRCYNWY in AAA34625. Ref.1

Sequence conflict

407 – 425

19

TFHTD…LMNES → IFTRTRFLYRFWPTNE in AAA34625. Ref.1

Secondary structure

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520

Helix Strand Turn

Details...

Beta strand

7 – 9

3

Helix

20 – 34

15

Beta strand

39 – 51

13

Helix

56 – 58

3

Beta strand

62 – 77

16

Beta strand

84 – 91

8

Beta strand

97 – 100

4

Beta strand

112 – 114

3

Helix

119 – 135

17

Helix

137 – 140

4

Beta strand

141 – 143

3

Beta strand

148 – 154

7

Helix

162 – 179

18

Helix

187 – 195

9

Helix

198 – 201

4

Helix

208 – 215

8

Beta strand

220 – 225

6

Beta strand

227 – 229

3

Beta strand

231 – 236

6

Beta strand

244 – 251

8

Helix

258 – 261

4

Turn

263 – 265

3

Helix

266 – 283

18

Beta strand

296 – 299

4

Helix

302 – 313

12

Helix

324 – 342

19

Helix

343 – 345

3

Helix

351 – 357

7

Helix

362 – 369

8

Beta strand

370 – 373

4

Beta strand

378 – 380

3

Helix

382 – 404

23

Helix

411 – 431

21

Helix

438 – 449

12

Beta strand

453 – 473

21

Helix

478 – 488

11

Helix

490 – 493

4

Helix

499 – 505

7

Beta strand

506 – 509

4

Beta strand

515 – 519

5

Sequences

	Sequence		Length	Mass (Da)
	P13045 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 5852028EBDDC0F3B	FASTA	520	58,129
	10 20 30 40 50 60 MNTNVPIFSS PVRDLPRSFE QKHLAVVDAF FQTYHVKPDF IARSPGRVNL IGEHIDYCDF 70 80 90 100 110 120 SVLPLAIDVD MLCAVKILDE KNPSITLTNA DPKFAQRKFD LPLDGSYMAI DPSVSEWSNY 130 140 150 160 170 180 FKCGLHVAHS YLKKIAPERF NNTPLVGAQI FCQSDIPTGG GLSSAFTCAA ALATIRANMG 190 200 210 220 230 240 KNFDISKKDL TRITAVAEHY VGVNNGGMDQ ATSVYGEEDH ALYVEFRPKL KATPFKFPQL 250 260 270 280 290 300 KNHEISFVIA NTLVKSNKFE TAPTNYNLRV IEVTVAANAL ATRYSVALPS HKDNSNSERG 310 320 330 340 350 360 NLRDFMDAYY ARYENQAQPW NGDIGTGIER LLKMLQLVEE SFSRKKSGFT VHEASTALNC 370 380 390 400 410 420 SREEFTRDYL TTFPVRFQVL KLYQRAKHVY SESLRVLKAL KMMTSATFHT DEDFFTDFGR 430 440 450 460 470 480 LMNESQASCD KLYECSCIET NQICSIALAN GSFGSRLTGA GWGGCTIHLV PSGANGNVEQ 490 500 510 520 VRKALIEKFY NVRYPDLTDE ELKDAIIVSK PALGTCLYEQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Yeast regulatory gene GAL3: carbon regulation; UASGal elements in common with GAL1, GAL2, GAL7, GAL10, GAL80, and MEL1; encoded protein strikingly similar to yeast and Escherichia coli galactokinases." Bajwa W., Torchia T.E., Hopper J.E. Mol. Cell. Biol. 8:3439-3447(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-425.
[2]	"Sequencing and analysis of a 35.4 kb region on the right arm of chromosome IV from Saccharomyces cerevisiae reveal 23 open reading frames." Eide L.G., Sander C., Prydz H. Yeast 12:1085-1090(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M21615 Genomic DNA. Translation: AAA34625.1.
X95966 Genomic DNA. Translation: CAA65201.1.
Z48008 Genomic DNA. Translation: CAA88069.1.
Z74305 Genomic DNA. Translation: CAA98829.1.
AY723766 Genomic DNA. Translation: AAU09683.1.
BK006938 Genomic DNA. Translation: DAA11856.1.

PIR

S50990.

RefSeq

NP_010292.1. NM_001180317.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3V2U	X-ray	2.10	C/D	2-520	[»]
3V5R	X-ray	2.10	A/B	17-520	[»]

ProteinModelPortal

P13045.

SMR

P13045. Positions 2-520.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5725N.

IntAct

P13045. 3 interactions.

MINT

MINT-4480213.

STRING

4932.YDR009W.

Proteomic databases

PaxDb

P13045.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR009W; YDR009W; YDR009W.

GeneID

851572.

KEGG

sce:YDR009W.

Organism-specific databases

CYGD

YDR009w.

SGD

S000002416. GAL3.

Phylogenomic databases

eggNOG

COG0153.

GeneTree

ENSGT00530000063433.

HOGENOM

HOG000241099.

KO

K00849.

OMA

MAMENET.

OrthoDB

EOG4GTPNF.

Gene expression databases

Genevestigator

P13045.

GermOnline

YDR009W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.30.230.10. 1 hit.

InterPro

IPR000705. Galactokinase.
IPR019741. Galactokinase_CS.
IPR019539. GalKase_gal-bd.
IPR013750. GHMP_kinase_C_dom.
IPR006204. GHMP_kinase_N_dom.
IPR006206. Mevalonate/galactokinase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]

Pfam

PF10509. GalKase_gal_bdg. 1 hit.
PF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000530. Galactokinase. 1 hit.

PRINTS

PR00473. GALCTOKINASE.
PR00959. MEVGALKINASE.

SUPFAM

SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.

TIGRFAMs

TIGR00131. gal_kin. 1 hit.

PROSITE

PS00106. GALACTOKINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

969025.

Entry information

Entry name

GAL3_YEAST

Accession

Primary (citable) accession number: P13045
Secondary accession number(s): D6VRZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program