Q8Y672 (KGUA_LISMO) 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:	gmk
Ordered Locus Names:	lmo1827

Organism

Listeria monocytogenes

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for recycling GMP and indirectly, cGMP By similarity. HAMAP MF_00328
Catalytic activity	ATP + GMP = ADP + GDP. HAMAP MF_00328
Subcellular location	Cytoplasm By similarity HAMAP MF_00328.
Sequence similarities	Belongs to the guanylate kinase family. Contains 1 guanylate kinase-like domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	purine nucleotide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW guanylate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 205

205

Guanylate kinase HAMAP MF_00328

PRO_0000170558

Regions

Domain

5 – 184

180

Guanylate kinase-like

Nucleotide binding

12 – 19

8

ATP By similarity

Secondary structure

1

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205

Helix Strand Turn

Details...

Beta strand

7 – 11

5

Helix

18 – 27

10

Beta strand

39 – 42

4

Turn

50 – 52

3

Helix

59 – 67

9

Beta strand

71 – 77

7

Beta strand

80 – 85

6

Helix

86 – 94

9

Beta strand

99 – 102

4

Helix

105 – 114

10

Beta strand

118 – 124

7

Turn

126 – 130

5

Helix

144 – 159

16

Helix

160 – 162

3

Beta strand

163 – 168

6

Helix

172 – 187

16

Helix

190 – 200

11

Sequences

	Sequence		Length	Mass (Da)
	Q8Y672 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 40579D7F0038C9E1	FASTA	205	23,282
	10 20 30 40 50 60 MTERGLLIVL SGPSGVGKGT VREAVFKDPE TSFDYSISMT TRLPREGEQD GVDYYFRSRE 70 80 90 100 110 120 VFEQAIKDGK MLEYAEYVGN YYGTPLEYVE EKLAAGVDIF LEIEVQGAMQ VRKAMPEGIF 130 140 150 160 170 180 IFLTPPDLSE LKNRIIGRGT ESMEVVEERM ETAKKEIEMM ASYDYAVVND VVANAVQKIK 190 200 GIVETEHLKT ERVIHRYKKM LEGLQ

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a.

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Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL591981 Genomic DNA. Translation: CAC99905.1.

PIR

AC1303.

RefSeq

NP_465352.1. NC_003210.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3TAU	X-ray	2.05	A/B	1-205	[»]

ProteinModelPortal

Q8Y672.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

985464.

GenomeReviews

Gene locus lmo1827 in contig AL591824_GR.

KEGG

lmo:lmo1827.

PATRIC

20312847. VBILisMon69206_1872.

Organism-specific databases

GenoList

LMO1827.

Phylogenomic databases

HOGENOM

HBG671982.

OMA

DIDWQGT.

ProtClustDB

PRK00300.

Enzyme and pathway databases

BioCyc

LMON169963:LMO1827-MONOMER.

Family and domain databases

HAMAP

MF_00328. Guanylate_kinase.
[Tree]

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...

Entry information

Entry name

KGUA_LISMO

Accession

Primary (citable) accession number: Q8Y672

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2002
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program