Q2GLF7 (KGUA_ANAPZ) 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:	APH_0170

Organism

Anaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP]

Taxonomic identifier

212042 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group › Anaplasma phagocytophilum

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for recycling GMP and indirectly, cGMP By similarity. HAMAP-Rule MF_00328
Catalytic activity	ATP + GMP = ADP + GDP. HAMAP-Rule MF_00328
Subcellular location	Cytoplasm By similarity.
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
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 – 210

210

Guanylate kinase HAMAP-Rule MF_00328

PRO_0000266285

Regions

Domain

6 – 186

181

Guanylate kinase-like

Nucleotide binding

13 – 20

8

ATP By similarity

Secondary structure

1

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210

Helix Strand Turn

Details...

Beta strand

8 – 12

5

Helix

22 – 27

6

Beta strand

34 – 36

3

Beta strand

40 – 43

4

Turn

51 – 53

3

Helix

60 – 68

9

Beta strand

72 – 78

7

Beta strand

81 – 86

6

Helix

90 – 96

7

Beta strand

99 – 103

5

Helix

106 – 115

10

Helix

117 – 119

3

Beta strand

120 – 126

7

Helix

130 – 135

6

Helix

152 – 159

8

Helix

160 – 164

5

Beta strand

165 – 170

6

Helix

174 – 189

16

Helix

192 – 194

3

Beta strand

195 – 197

3

Helix

198 – 205

8

Sequences

	Sequence		Length	Mass (Da)
	Q2GLF7 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: A49B447B562D4E93	FASTA	210	23,928
	10 20 30 40 50 60 MLKSVGVILV LSSPSGCGKT TVANKLLEKQ KNNIVKSVSV TTRAARKGEK EGKDYYFVDR 70 80 90 100 110 120 EEFLRLCSNG EIIEHAEVFG NFYGVPRKNL EDNVDKGVST LLVIDWQGAF KFMEMMREHV 130 140 150 160 170 180 VSIFIMPPSM EELRRRLCGR RADDSEVVEA RLKGAAFEIS HCEAYDYVIV NEDIEETADR 190 200 210 ISNILRAEQM KTCRQVGLRE LLESRFPIED

References

[1]

"Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. , Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H. PLoS Genet. 2:208-222(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HZ.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000235 Genomic DNA. Translation: ABD43557.1.

RefSeq

YP_504794.1. NC_007797.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LNC	X-ray	1.95	A/B	1-210	[»]

ProteinModelPortal

Q2GLF7.

ModBase

Search...

Protein-protein interaction databases

STRING

212042.APH_0170.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

ABD43557; ABD43557; APH_0170.

GeneID

3930277.

KEGG

aph:APH_0170.

PATRIC

20948908. VBIAnaPha602_0179.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0194.

HOGENOM

HOG000037638.

KO

K00942.

OMA

FVIINEL.

ProtClustDB

PRK00300.

Enzyme and pathway databases

BioCyc

APHA212042:GHPM-205-MONOMER.

Family and domain databases

HAMAP

MF_00328. Guanylate_kinase.

InterPro

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

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

EvolutionaryTrace

Q2GLF7.

Entry information

Entry name

KGUA_ANAPZ

Accession

Primary (citable) accession number: Q2GLF7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	March 21, 2006
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program