Q72NQ8 (PROB_LEPIC) 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:	LIC_12772

Organism

Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) [Complete proteome] [HAMAP]

Taxonomic identifier

267671 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Spirochaetes › Spirochaetia › Spirochaetales › Leptospiraceae › Leptospira › Leptospira interrogans › Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni

Protein attributes

Sequence length	290 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.

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 – 290	290	Glutamate 5-kinase HAMAP-Rule MF_00456		PRO_0000109685
Regions
	Nucleotide binding	217 – 223	7	ATP By similarity
Sites
	Binding site	21	1	ATP By similarity
	Binding site	60	1	Substrate By similarity
	Binding site	151	1	Substrate By similarity
	Binding site	163	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q72NQ8 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 24CB9C7E6A78E335	FASTA	290	31,307
	10 20 30 40 50 60 MKPERNSLSE KIRNAEKIVI KVGSARLSGL PSEVNDFLFQ LVSDIRHLRD LGKKVILVSS 70 80 90 100 110 120 GAIARGRLLL SELPSTISSG DSLAEKQALA AMGQNRLVNL YDSFFSKVNL SIAQILFGVL 130 140 150 160 170 180 DLESKEGYKN LKNTFTQLVE WGILPVVNEN DSVATEEVKF GDNDMLSALV SLIVEADLLI 190 200 210 220 230 240 ILTGVDGFLK EEKVVPFLEK ISKEDLGLAG GPSGPGTGGM FTKLKSAGLL SEAGIPTAIL 250 260 270 280 290 NGKKMHVIRE FLEKNSIGTL VAPSGNRVFS EEDVKEIIRK NRNGNGGNSL

References

[1]

"Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis." Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S. , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A. J. Bacteriol. 186:2164-2172(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Fiocruz L1-130.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016823 Genomic DNA. Translation: AAS71328.1.
RefSeq	YP_002691.1. NC_005823.1.
3D structure databases
ProteinModelPortal	Q72NQ8.
ModBase	Search...
Protein-protein interaction databases
STRING	267671.LIC12772.
Proteomic databases
PaxDb	Q72NQ8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAS71328; AAS71328; LIC_12772.
GeneID	2770261.
KEGG	lic:LIC12772.
PATRIC	22378369. VBILepInt6257_3338.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0263.
KO	K00931.
OMA	VYTGNPK.
ProtClustDB	PRK12314.
Enzyme and pathway databases
BioCyc	LINT267671:GHQI-2764-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

PROB_LEPIC

Accession

Primary (citable) accession number: Q72NQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	July 5, 2004
Last modified:	May 29, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program