Q57B46 (PROB_BRUAB) 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:	BruAb1_1823

Organism

Brucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]

Taxonomic identifier

262698 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella abortus › Brucella abortus bv. 1

Protein attributes

Sequence length	378 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 – 378	378	Glutamate 5-kinase HAMAP-Rule MF_00456		PRO_0000109651
Regions
	Domain	279 – 356	78	PUA
	Nucleotide binding	173 – 174	2	ATP By similarity
Sites
	Binding site	14	1	ATP By similarity
	Binding site	54	1	Substrate By similarity
	Binding site	141	1	Substrate By similarity
	Binding site	153	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q57B46 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: AB4866F6CEFF3D11	FASTA	378	39,873
	10 20 30 40 50 60 MLKKLKDYRR IVVKIGSALL VDRATGLKRK WLESLGQDIA ALQHAGVEVL VVSSGAIALG 70 80 90 100 110 120 RTVLGLPKKA LKLEESQAAA AAGQIALAKA YADVLGGHGI KSGQILVTLS DTEERRRYLN 130 140 150 160 170 180 ARATIETLLK LKAVPIINEN DTVATTEIRY GDNDRLAARV ATMMGADLLI LLSDIDGLYT 190 200 210 220 230 240 APPHKNPDAQ FLPFVETITP QIEAMAGAAA SELSRGGMKT KLDAGKIANA AGTAMIITSG 250 260 270 280 290 300 TRFGPLSAID RGERATLFEA AHAPVNAWKT WISGNLEPAG RLTVDAGAVK ALKSGKSLLP 310 320 330 340 350 360 AGVKEVDGDF ERGDTVAVMN EDGREIARGL IAYDAADARK VAGHKSDEIS AILGYDARAA 370 MIHRNDLVVR AASDAKAA

References

[1]

"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017223 Genomic DNA. Translation: AAX75138.1.
RefSeq	YP_222499.1. NC_006932.1.
3D structure databases
ProteinModelPortal	Q57B46.
ModBase	Search...
Protein-protein interaction databases
STRING	262698.BruAb1_1823.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAX75138; AAX75138; BruAb1_1823.
GeneID	3340401.
KEGG	bmb:BruAb1_1823.
PATRIC	17825451. VBIBruAbo15061_1927.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0263.
HOGENOM	HOG000246368.
KO	K00931.
OMA	DHLQLRG.
ProtClustDB	PRK05429.
Enzyme and pathway databases
BioCyc	BABO262698:GJC2-1863-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. 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_BRUAB

Accession

Primary (citable) accession number: Q57B46

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program