C3M9Y0 (PROB_RHISN) 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:	NGR_c31710

Organism

Rhizobium sp. (strain NGR234) [Complete proteome] [HAMAP]

Taxonomic identifier

394 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium › Sinorhizobium fredii group › Rhizobium fredii

Protein attributes

Sequence length	393 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 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	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 – 393	393	Glutamate 5-kinase HAMAP-Rule MF_00456		PRO_1000193701
Regions
	Domain	282 – 359	78	PUA
	Nucleotide binding	176 – 177	2	ATP By similarity
Sites
	Binding site	17	1	ATP By similarity
	Binding site	57	1	Substrate By similarity
	Binding site	144	1	Substrate By similarity
	Binding site	156	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	C3M9Y0 [UniParc]. Last modified June 16, 2009. Version 1. Checksum: 61AFEE1D959CF135	FASTA	393	41,020
	10 20 30 40 50 60 MAATVRPLEK YRRIVIKIGS ALLVDRKSGL KKSWLDAMCV DIAALKAKGV EVLVVSSGAI 70 80 90 100 110 120 ALGRTVLNLP AGALKLEESQ AAAAVGQIAL ARAWSESLST DQIIAGQILL TLGDTEERRR 130 140 150 160 170 180 YLNARATINQ LLKLGSVPII NENDTVATTE IRYGDNDRLA ARVATMVGAD LLVLLSDIDG 190 200 210 220 230 240 LYTAPPHLDP QARFLETIAE ITPEIEAMAG GAASELSRGG MRTKIDAGKI ATTAGCAMII 250 260 270 280 290 300 ASGKPEHPLK AIEAGARSSW FAPSGSPVTA RKTWIAGQLL PAGSIAIDAG AETALRSGKS 310 320 330 340 350 360 LLPAGVRQVT GTFSRGDTIA ILNASGREIA RGLAGYDADD ARQIAGKKSA EIAAILGYAG 370 380 390 RTAMVHRDDM VMTAPSGARS EEGGNEKKGK LHA

References

[1]

"Rhizobium sp. strain NGR234 possesses a remarkable number of secretion systems." Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A., Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A., Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A., Broughton W.J., Perret X., Strittmatter A.W., Streit W.R. Appl. Environ. Microbiol. 75:4035-4045(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NGR234.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001389 Genomic DNA. Translation: ACP26905.1.
RefSeq	YP_002827658.1. NC_012587.1.
3D structure databases
ProteinModelPortal	C3M9Y0.
ModBase	Search...
Protein-protein interaction databases
STRING	394.NGR_c31710.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACP26905; ACP26905; NGR_c31710.
GeneID	7792441.
KEGG	rhi:NGR_c31710.
PATRIC	32312857. VBIRhiSp122450_6009.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0263.
HOGENOM	HOG000246368.
KO	K00931.
OMA	DHLQLRG.
ProtClustDB	PRK05429.
Enzyme and pathway databases
BioCyc	SFRE394:GBYN-3158-MONOMER.
UniPathway	UPA00098; UER00359.
Family and domain databases
Gene3D	2.30.130.10. 1 hit. 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_RHISN

Accession

Primary (citable) accession number: C3M9Y0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	June 16, 2009
Last modified:	May 29, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program