Q92LF7 (PROB2_RHIME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate 5-kinase 2
EC=2.7.2.11

Alternative name(s):
Gamma-glutamyl kinase 2
Short name=GK 2

Gene names

Name:	proB2
Ordered Locus Names:	R03106
ORF Names:	SMc03252

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	269 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.
Sequence caution	The sequence CAC47685.1 differs from that shown. Reason: Erroneous initiation.

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 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 – 269	269	Glutamate 5-kinase 2 HAMAP-Rule MF_00456		PRO_0000109716
Regions
	Nucleotide binding	218 – 224	7	ATP By similarity
Sites
	Binding site	16	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)
	Q92LF7 [UniParc]. Last modified July 26, 2002. Version 2. Checksum: 9DE5148CA9ECB292	FASTA	269	28,953
	10 20 30 40 50 60 MEDKFDLSSA RLVVVKIGST LVLDRETSGI RSSWLESLTE DVSRLLTRGQ QVVLVSSGAV 70 80 90 100 110 120 AIGSTIVDRL ATYSQVSHKQ AAAALGQVQL THAYSESLKR HGLQVAQLLM GRGDLVDPAH 130 140 150 160 170 180 RLNTRAVLLR LIDLGAVPLV NENDTTATCG TRVGDNDRLA AWIAEIINAD LLILLSNVDG 190 200 210 220 230 240 LFMKDPRNNP LTPMLTEVES ITREIEAMAT QSVDPYSSGG MISKIEAGKI AMNAGCRMII 250 260 ANGTRSHPLY AIESGGPSTH FIPVARDRV

References

[1]

"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

[2]

"The composite genome of the legume symbiont Sinorhizobium meliloti." Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J. Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591688 Genomic DNA. Translation: CAC47685.1. Different initiation.
RefSeq	NP_387212.1. NC_003047.1.
3D structure databases
ProteinModelPortal	Q92LF7.
ModBase	Search...
Protein-protein interaction databases
STRING	266834.SMc03252.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC47685; CAC47685; SMc03252.
GeneID	1234791.
KEGG	sme:SMc03252.
PATRIC	23635840. VBISinMel96828_4643.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0263.
HOGENOM	HOG000246368.
KO	K00931.
ProtClustDB	PRK12314.
Enzyme and pathway databases
BioCyc	SMEL266834:GJF6-3185-MONOMER.
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. [Graphical view]
Pfam	PF00696. AA_kinase. 1 hit. [Graphical view]
PIRSF	PIRSF000729. GK. 1 hit.
PRINTS	PR00474. GLU5KINASE.
SUPFAM	SSF53633. Aa_kinase. 1 hit.
TIGRFAMs	TIGR01027. proB. 1 hit.
PROSITE	PS00902. GLUTAMATE_5_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PROB2_RHIME

Accession

Primary (citable) accession number: Q92LF7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	July 26, 2002
Last modified:	May 1, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program