P71910 (PROB_MYCTU) 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:	Rv2439c, MT2515
ORF Names:	MTCY428.07

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	376 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.
Miscellaneous	Was identified as a high-confidence drug target. 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 Reference proteome
Gene Ontology (GO)
Biological_process	L-proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway growth Inferred from mutant phenotype PubMed 12657046. Source: MTBBASE
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 – 376	376	Glutamate 5-kinase HAMAP-Rule MF_00456		PRO_0000109696
Regions
	Domain	280 – 358	79	PUA
	Nucleotide binding	177 – 178	2	ATP By similarity
	Nucleotide binding	218 – 224	7	ATP By similarity
Sites
	Binding site	18	1	ATP By similarity
	Binding site	58	1	Substrate By similarity
	Binding site	145	1	Substrate By similarity
	Binding site	157	1	Substrate; via amide nitrogen By similarity
Experimental info
	Sequence conflict	226	1	A → S in AAK46812. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P71910 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: AC7BB66C0B302E6A	FASTA	376	38,788
	10 20 30 40 50 60 MRSPHRDAIR TARGLVVKVG TTALTTPSGM FDAGRLAGLA EAVERRMKAG SDVVIVSSGA 70 80 90 100 110 120 IAAGIEPLGL SRRPKDLATK QAAASVGQVA LVNSWSAAFA RYGRTVGQVL LTAHDISMRV 130 140 150 160 170 180 QHTNAQRTLD RLRALHAVAI VNENDTVATN EIRFGDNDRL SALVAHLVGA DALVLLSDID 190 200 210 220 230 240 GLYDCDPRKT ADATFIPEVS GPADLDGVVA GRSSHLGTGG MASKVAAALL AADAGVPVLL 250 260 270 280 290 300 APAADAATAL ADASVGTVFA ARPARLSARR FWVRYAAEAT GALTLDAGAV RAVVRQRRSL 310 320 330 340 350 360 LAAGITAVSG RFCGGDVVEL RAPDAAMVAR GVVAYDASEL ATMVGRSTSE LPGELRRPVV 370 HADDLVAVSA KQAKQV

References

[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis." Raman K., Yeturu K., Chandra N. BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842579 Genomic DNA. Translation: CAB03780.1. AE000516 Genomic DNA. Translation: AAK46812.1. AL123456 Genomic DNA. Translation: CCP45232.1.
PIR	E70680.
RefSeq	NP_216955.1. NC_000962.3. NP_336998.1. NC_002755.2. YP_006515876.1. NC_018143.1.
3D structure databases
ProteinModelPortal	P71910.
SMR	P71910. Positions 12-366.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv2439c.
Proteomic databases
PRIDE	P71910.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK46812; AAK46812; MT2515.
GeneID	13319149. 885266. 925792.
KEGG	mtc:MT2515. mtu:Rv2439c. mtv:RVBD_2439c.
PATRIC	18127280. VBIMycTub22151_2748.
Organism-specific databases
TubercuList	Rv2439c.
Phylogenomic databases
eggNOG	COG0263.
HOGENOM	HOG000246368.
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_MYCTU

Accession

Primary (citable) accession number: P71910
Secondary accession number(s): L0TCJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program