B7N8H3 (PROB_ECOLU) 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:	ECUMN_0308

Organism

Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

585056 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline By similarity. 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
Subcellular location	Cytoplasm By similarity.
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	Complete proteome
Gene Ontology (GO)
Biological_process	L-proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 electronic annotation. Source: HAMAP
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_1000125233
Regions
	Domain	275 – 353	79	PUA
	Nucleotide binding	169 – 170	2	ATP By similarity
	Nucleotide binding	211 – 217	7	ATP By similarity
Sites
	Binding site	10	1	ATP By similarity
	Binding site	50	1	Substrate By similarity
	Binding site	137	1	Substrate By similarity
	Binding site	149	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7N8H3 [UniParc]. Last modified March 24, 2009. 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

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UMN026 / ExPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928163 Genomic DNA. Translation: CAR11523.1.
RefSeq	YP_002411077.1. NC_011751.1.
3D structure databases
ProteinModelPortal	B7N8H3.
SMR	B7N8H3. Positions 3-367.
ModBase	Search...
Protein-protein interaction databases
STRING	585056.ECUMN_0308.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAR11523; CAR11523; ECUMN_0308.
GeneID	7157457.
KEGG	eum:ECUMN_0308.
PATRIC	18439833. VBIEscCol32010_0503.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0263.
HOGENOM	HOG000246369.
KO	K00931.
OMA	DHLQLRG.
ProtClustDB	PRK05429.
Enzyme and pathway databases
UniPathway	UPA00098; UER00359.
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...

Entry information

Entry name

PROB_ECOLU

Accession

Primary (citable) accession number: B7N8H3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	March 24, 2009
Last modified:	May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program