P15454 (KGUA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanylate kinase
EC=2.7.4.8

Alternative name(s):
GMP kinase

Gene names

Name:	GUK1
Ordered Locus Names:	YDR454C
ORF Names:	D9461.39

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for recycling GMP and indirectly, cGMP.
Catalytic activity	ATP + GMP = ADP + GDP.
Subunit structure	Monomer.
Miscellaneous	Present with 20500 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the guanylate kinase family. Contains 1 guanylate kinase-like domain.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	GMP metabolic process Traceable author statement. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW guanylate kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-9672,EBI-9672
ACF2	Q12168	1	EBI-9672,EBI-32973
UBX2	Q04228	1	EBI-9672,EBI-27730

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 187

186

Guanylate kinase

PRO_0000170655

Regions

Domain

2 – 184

183

Guanylate kinase-like

Nucleotide binding

9 – 16

8

ATP

Nucleotide binding

35 – 82

48

GMP

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.11

Modified residue

149

1

Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

187

Helix Strand Turn

Details...

Beta strand

5 – 8

4

Helix

15 – 25

11

Turn

27 – 29

3

Turn

47 – 49

3

Helix

56 – 64

9

Beta strand

68 – 74

7

Beta strand

77 – 82

6

Helix

83 – 91

9

Beta strand

94 – 99

6

Helix

102 – 109

8

Beta strand

117 – 122

6

Helix

126 – 136

11

Helix

142 – 158

17

Turn

159 – 161

3

Beta strand

163 – 168

6

Helix

172 – 183

12

Sequences

	Sequence		Length	Mass (Da)
	P15454 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 5DC4D2A22594BFB8	FASTA	187	20,637
	10 20 30 40 50 60 MSRPIVISGP SGTGKSTLLK KLFAEYPDSF GFSVSSTTRT PRAGEVNGKD YNFVSVDEFK 70 80 90 100 110 120 SMIKNNEFIE WAQFSGNYYG STVASVKQVS KSGKTCILDI DMQGVKSVKA IPELNARFLF 130 140 150 160 170 180 IAPPSVEDLK KRLEGRGTET EESINKRLSA AQAELAYAET GAHDKVIVND DLDKAYKELK DFIFAEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of the essential gene for guanylate kinase from yeast." Konrad M. J. Biol. Chem. 267:25652-25655(1992) [PubMed: 1334480] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Guanylate kinase from Saccharomyces cerevisiae. Isolation and characterization, crystallization and preliminary X-ray analysis, amino acid sequence and comparison with adenylate kinases." Berger A., Schiltz E., Schulz G.E. Eur. J. Biochem. 184:433-443(1989) [PubMed: 2551688] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-187.
[5]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, MASS SPECTROMETRY. Strain: ADR376.
[7]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, MASS SPECTROMETRY.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, MASS SPECTROMETRY.
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, MASS SPECTROMETRY.
[10]	"Three-dimensional structure of the complex of guanylate kinase from yeast with its substrate GMP." Stehle T., Schulz G.E. J. Mol. Biol. 211:249-254(1990) [PubMed: 1967656] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[11]	"Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0-A resolution." Stehle T., Schulz G.E. J. Mol. Biol. 224:1127-1141(1992) [PubMed: 1314905] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L04683 Genomic DNA. Translation: AAA34657.1.
U33007 Genomic DNA. Translation: AAB64881.1.
BK006938 Genomic DNA. Translation: DAA12289.1.

PIR

KIBYGU. A45097.

RefSeq

NP_010742.1. NM_001180762.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EX6	X-ray	2.30	A/B	2-186	[»]
1EX7	X-ray	1.90	A	2-186	[»]
1GKY	X-ray	2.00	A	2-187	[»]
3SQK	X-ray	2.45	A/B	1-187	[»]

ProteinModelPortal

P15454.

SMR

P15454. Positions 2-187.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6721N.

IntAct

P15454. 4 interactions.

MINT

MINT-522729.

STRING

P15454.

Proteomic databases

PeptideAtlas

P15454.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR454C; YDR454C; YDR454C.

GeneID

852065.

KEGG

sce:YDR454C.

NMPDR

fig|4932.3.peg.1515.

Organism-specific databases

SGD

S000002862. GUK1.

Phylogenomic databases

eggNOG

fuNOG05067.

GeneTree

EFGT00050000001116.

HOGENOM

HBG671982.

OMA

PDKFGFS.

OrthoDB

EOG4FR41X.

Gene expression databases

ArrayExpress

P15454.

Genevestigator

P15454.

GermOnline

YDR454C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR008144. Guanylate_kin.
IPR008145. Guanylate_kin/L-typ_Ca_channel.
IPR020590. Guanylate_kinase_CS.
IPR017665. Guanylate_kinase_sub.
[Graphical view]

KO

K00942.

Pfam

PF00625. Guanylate_kin. 1 hit.
[Graphical view]

SMART

SM00072. GuKc. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03263. Guanyl_kin. 1 hit.

PROSITE

PS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

970349.

Entry information

Entry name

KGUA_YEAST

Accession

Primary (citable) accession number: P15454
Secondary accession number(s): D6VT79

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program