O58328 (GLKA_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ADP-dependent glucokinase
Short name=ADP-GK
Short name=ADPGK
EC=2.7.1.147

Gene names

Name:	glkA
Ordered Locus Names:	PH0589

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. HAMAP MF_00809
Catalytic activity	ADP + D-glucose = AMP + D-glucose 6-phosphate. HAMAP MF_00809
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00809
Pathway	Carbohydrate degradation; glycolysis. HAMAP MF_00809
Subunit structure	Monomer.
Subcellular location	Cytoplasm By similarity HAMAP MF_00809.
Sequence similarities	Belongs to the ADP-dependent glucokinase family. Contains 1 ADPK (ADP-dependent kinase) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism Glycolysis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ADP-specific glucokinase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 457

457

ADP-dependent glucokinase HAMAP MF_00809

PRO_0000184773

Regions

Domain

5 – 457

453

ADPK

Nucleotide binding

345 – 347

3

ADP By similarity

Nucleotide binding

441 – 445

5

ADP By similarity

Sites

Active site

443

1

Proton acceptor By similarity

Metal binding

269

1

Magnesium By similarity

Metal binding

298

1

Magnesium By similarity

Metal binding

443

1

Magnesium By similarity

Binding site

33

1

Glucose By similarity

Binding site

37

1

Glucose By similarity

Binding site

91

1

Glucose By similarity

Binding site

116

1

Glucose By similarity

Binding site

179

1

Glucose By similarity

Binding site

200

1

Glucose By similarity

Binding site

295

1

ADP By similarity

Binding site

345

1

ADP By similarity

Binding site

346

1

ADP; via carbonyl oxygen By similarity

Binding site

432

1

ADP; via carbonyl oxygen By similarity

Binding site

443

1

ADP By similarity

Binding site

443

1

Glucose By similarity

Secondary structure

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457

Helix Strand Turn

Details...

Helix

8 – 21

14

Helix

22 – 24

3

Beta strand

28 – 32

5

Beta strand

35 – 39

5

Helix

44 – 54

11

Helix

56 – 64

9

Beta strand

68 – 70

3

Helix

73 – 86

14

Beta strand

90 – 94

5

Helix

97 – 106

10

Beta strand

109 – 115

7

Helix

116 – 124

9

Turn

125 – 127

3

Beta strand

132 – 134

3

Helix

141 – 145

5

Beta strand

149 – 155

7

Helix

167 – 169

3

Beta strand

178 – 180

3

Beta strand

199 – 205

7

Helix

209 – 211

3

Helix

216 – 220

5

Helix

222 – 226

5

Beta strand

230 – 235

6

Turn

242 – 244

3

Helix

246 – 261

16

Beta strand

265 – 269

5

Helix

276 – 285

10

Helix

286 – 288

3

Beta strand

290 – 294

5

Helix

296 – 305

10

Helix

309 – 317

9

Beta strand

318 – 320

3

Helix

323 – 337

15

Beta strand

340 – 346

7

Beta strand

349 – 356

8

Helix

360 – 378

19

Helix

384 – 392

9

Helix

397 – 409

13

Beta strand

416 – 419

4

Beta strand

422 – 428

7

Helix

443 – 456

14

Sequences

	Sequence		Length	Mass (Da)
	O58328 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: A30EF1398FA9BC94	FASTA	457	52,090
	10 20 30 40 50 60 MITMTNWESL YEKALDKVEA SIRKVRGVLL AYNTNIDAIK YLKREDLEKR IEKVGKEEVL 70 80 90 100 110 120 RYSEELPKEI ETIPQLLGSI LWSIKRGKAA ELLVVSREVR EYMRKWGWDE LRMGGQVGIM 130 140 150 160 170 180 ANLLGGVYGI PVIAHVPQLS ELQASLFLDG PIYVPTFERG ELRLIHPREF RKGEEDCIHY 190 200 210 220 230 240 IYEFPRNFKV LDFEAPRENR FIGAADDYNP ILYVREEWIE RFEEIAKRSE LAIISGLHPL 250 260 270 280 290 300 TQENHGKPIK LVREHLKILN DLGIRAHLEF AFTPDEVVRL EIVKLLKHFY SVGLNEVELA 310 320 330 340 350 360 SVVSVMGEKE LAERIISKDP ADPIAVIEGL LKLIKETGVK RIHFHTYGYY LALTREKGEH 370 380 390 400 410 420 VRDALLFSAL AAATKAMKGN IEKLSDIREG LAVPIGEQGL EVEKILEKEF SLRDGIGSIE 430 440 450 DYQLTFIPTK VVKKPKSTVG IGDTISSSAF VSEFSLH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[2]	"Crystal structure of the ADP-dependent glucokinase from Pyrococcus horikoshii at 2.0-A resolution: a large conformational change in ADP-dependent glucokinase." Tsuge H., Sakuraba H., Kobe T., Kujime A., Katunuma N., Ohshima T. Protein Sci. 11:2456-2463(2002) [PubMed: 12237466] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. Translation: BAA29678.1.

PIR

A71174.

RefSeq

NP_142553.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L2L	X-ray	2.00	A	1-457	[»]

ProteinModelPortal

O58328.

SMR

O58328. Positions 7-457.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000001248; EBPYRP00000001248; EBPYRG00000001248.

GeneID

1442924.

GenomeReviews

Gene locus PH0589 in contig BA000001_GR.

KEGG

pho:PH0589.

NMPDR

fig|70601.1.peg.577.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000022952.

HOGENOM

HBG645711.

OMA

IHYIYEF.

ProtClustDB

PRK14038.

Enzyme and pathway databases

BioCyc

PHOR70601:PH0589-MONOMER.

Family and domain databases

HAMAP

MF_00809. ADP_glucokinase.
[Tree]

InterPro

IPR007666. ADP_PFK/GK.
IPR015990. ADP_PFK/GK_arc.
[Graphical view]

KO

K00918.

Pfam

PF04587. ADP_PFK_GK. 1 hit.
[Graphical view]

PIRSF

PIRSF015883. ADP-Pfk_glckin. 1 hit.

PROSITE

PS51255. ADPK. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GLKA_PYRHO

Accession

Primary (citable) accession number: O58328

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	August 1, 1998
Last modified:	November 16, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program