P0A7B5 (PROB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate 5-kinase
EC=2.7.2.11

Alternative name(s):
Gamma-glutamyl kinase
Short name=GK

Gene names

Name:	proB
Ordered Locus Names:	b0242, JW0232

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline. HAMAP-Rule MF_00456
Catalytic activity	ATP + L-glutamate = ADP + L-glutamate 5-phosphate. HAMAP-Rule MF_00456
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. HAMAP-Rule MF_00456
Subunit structure	Homotetramer. Dimer of dimers. Ref.7
Subcellular location	Cytoplasm HAMAP-Rule MF_00456.
Sequence similarities	Belongs to the glutamate 5-kinase family. Contains 1 PUA domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Proline biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway proline biosynthetic process Inferred from mutant phenotype PubMed 2841193. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: InterPro glutamate 5-kinase activity Inferred from direct assay PubMed 16337196PubMed 17069808PubMed 6319365. Source: EcoCyc magnesium ion binding Inferred from direct assay PubMed 16337196PubMed 17069808PubMed 6319365. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 367

367

Glutamate 5-kinase HAMAP-Rule MF_00456

PRO_0000109669

Regions

Domain

275 – 353

79

PUA

Nucleotide binding

169 – 170

2

ATP Probable

Nucleotide binding

211 – 217

7

ATP Probable

Sites

Binding site

10

1

ATP Probable

Binding site

50

1

Substrate

Binding site

137

1

Substrate

Binding site

149

1

Substrate; via amide nitrogen

Experimental info

Sequence conflict

143

1

E → A Ref.1

Sequence conflict

143

1

E → A Ref.2

Secondary structure

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367

Helix Strand Turn

Details...

Beta strand

6 – 11

6

Helix

13 – 16

4

Turn

17 – 19

3

Beta strand

20 – 22

3

Helix

25 – 40

16

Beta strand

44 – 49

6

Helix

52 – 60

9

Helix

69 – 92

24

Turn

93 – 95

3

Beta strand

98 – 103

6

Helix

105 – 108

4

Helix

111 – 126

16

Beta strand

130 – 135

6

Turn

137 – 139

3

Helix

142 – 144

3

Helix

149 – 160

12

Beta strand

163 – 169

7

Beta strand

175 – 177

3

Turn

179 – 181

3

Beta strand

190 – 193

4

Helix

194 – 196

3

Turn

197 – 199

3

Helix

215 – 226

12

Beta strand

230 – 235

6

Helix

241 – 247

7

Beta strand

252 – 255

4

Helix

264 – 270

7

Beta strand

277 – 280

4

Helix

282 – 291

10

Helix

297 – 299

3

Beta strand

300 – 305

6

Beta strand

312 – 317

6

Beta strand

322 – 327

6

Helix

332 – 338

7

Helix

343 – 345

3

Helix

346 – 350

5

Helix

361 – 363

3

Beta strand

364 – 366

3

Sequences

	Sequence		Length	Mass (Da)
	P0A7B5 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 5541040202EBCCE8	FASTA	367	39,057
	10 20 30 40 50 60 MSDSQTLVVK LGTSVLTGGS RRLNRAHIVE LVRQCAQLHA AGHRIVIVTS GAIAAGREHL 70 80 90 100 110 120 GYPELPATIA SKQLLAAVGQ SRLIQLWEQL FSIYGIHVGQ MLLTRADMED RERFLNARDT 130 140 150 160 170 180 LRALLDNNIV PVINENDAVA TAEIKVGDND NLSALAAILA GADKLLLLTD QKGLYTADPR 190 200 210 220 230 240 SNPQAELIKD VYGIDDALRA IAGDSVSGLG TGGMSTKLQA ADVACRAGID TIIAAGSKPG 250 260 270 280 290 300 VIGDVMEGIS VGTLFHAQAT PLENRKRWIF GAPPAGEITV DEGATAAILE RGSSLLPKGI 310 320 330 340 350 360 KSVTGNFSRG EVIRICNLEG RDIAHGVSRY NSDALRRIAG HHSQEIDAIL GYEYGPVAVH RDDMITR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli proBA locus by DNA and protein sequencing." Deutch A.H., Rushlow K.E., Smith C.J. Nucleic Acids Res. 12:6337-6355(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6 AND 8-12.
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region." Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 143. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Complete nucleotide sequence of phoE, the structural gene for the phosphate limitation inducible outer membrane pore protein of Escherichia coli K12." Overbeeke N., Bergmans H., van Mansfeld F., Lugtenberg B. J. Mol. Biol. 163:513-532(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62. Strain: K12.
[7]	"A novel two-domain architecture within the amino acid kinase enzyme family revealed by the crystal structure of Escherichia coli glutamate 5-kinase." Marco-Marin C., Gil-Ortiz F., Perez-Arellano I., Cervera J., Fita I., Rubio V. J. Mol. Biol. 367:1431-1446(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH 5-OXOPROLINE AND D-GAMMA-GLUTAMYL PHOSPHATE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X00786 Genomic DNA. Translation: CAA25363.1.
U70214 Genomic DNA. Translation: AAB08662.1.
U00096 Genomic DNA. Translation: AAC73346.1.
AP009048 Genomic DNA. Translation: BAA77911.2.
V00316 Genomic DNA. Translation: CAA23604.1.

PIR

KIECEG. C64749.

RefSeq

NP_414777.1. NC_000913.2.
YP_488537.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J5T	X-ray	2.90	A/B/C/D/E/F/G/H	1-367	[»]
2J5V	X-ray	2.50	A/B	1-367	[»]
2W21	X-ray	2.95	A	1-259	[»]

ProteinModelPortal

P0A7B5.

SMR

P0A7B5. Positions 3-367.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A7B5. 2 interactions.

STRING

511145.b0242.

Proteomic databases

PaxDb

P0A7B5.

PRIDE

P0A7B5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73346; AAC73346; b0242.
BAA77911; BAA77911; BAA77911.

GeneID

12930773.
946425.

KEGG

ecj:Y75_p0233.
eco:b0242.

PATRIC

32115599. VBIEscCol129921_0244.

Organism-specific databases

EchoBASE

EB0761.

EcoGene

EG10768. proB.

Phylogenomic databases

eggNOG

COG0263.

HOGENOM

HOG000246369.

KO

K00931.

OMA

DHLQLRG.

ProtClustDB

PRK05429.

Enzyme and pathway databases

BioCyc

EcoCyc:GLUTKIN-MONOMER.
ECOL316407:JW0232-MONOMER.
MetaCyc:GLUTKIN-MONOMER.

BRENDA

2.7.2.11. 2026.

SABIO-RK

P0A7B5.

UniPathway

UPA00098; UER00359.

Gene expression databases

Genevestigator

P0A7B5.

Family and domain databases

Gene3D

3.40.1160.10. 1 hit.

HAMAP

MF_00456. ProB.

InterPro

IPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
IPR011529. Glu_5kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
IPR002478. PUA.
IPR015947. PUA-like_domain.
[Graphical view]

Pfam

PF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]

PIRSF

PIRSF000729. GK. 1 hit.

PRINTS

PR00474. GLU5KINASE.

SMART

SM00359. PUA. 1 hit.
[Graphical view]

SUPFAM

SSF53633. Aa_kinase. 1 hit.
SSF88697. PUA-like. 1 hit.

TIGRFAMs

TIGR01027. proB. 1 hit.

PROSITE

PS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7B5.

Entry information

Entry name

PROB_ECOLI

Accession

Primary (citable) accession number: P0A7B5
Secondary accession number(s): P07005, P78293

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program