Q60050 (PROB_THET2) 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:	TT_C1563

Organism

Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP]

Taxonomic identifier

262724 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	370 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 – 370	370	Glutamate 5-kinase HAMAP-Rule MF_00456		PRO_0000109747
Regions
	Domain	275 – 353	79	PUA
	Nucleotide binding	171 – 172	2	ATP By similarity
	Nucleotide binding	211 – 217	7	ATP By similarity
Sites
	Binding site	13	1	ATP By similarity
	Binding site	52	1	Substrate By similarity
	Binding site	139	1	Substrate By similarity
	Binding site	151	1	Substrate; via amide nitrogen By similarity
Experimental info
	Sequence conflict	1 – 32	32	MRPGL…EAMAE → MEFFGLPLRVEEGVLIPRPE TEGLVELALGLPLPPAPR Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q60050 [UniParc]. Last modified May 24, 2004. Version 2. Checksum: 8B67CD67D2A057BB	FASTA	370	39,890
	10 20 30 40 50 60 MRPGLSAKRL VVKVGSAVLT GERGLDLEAM AEIARQVAAL REEGREVVLV SSGAVAAGMR 70 80 90 100 110 120 RLGLKERPKD MPKKQALAAL GQPLLMAFWQ EAFAPFGLPV AQVLLTAEDL SSRSRYLNAK 130 140 150 160 170 180 ATLRALLDLG AIPVINENDT VAFEEIRFGD NDQLSARVAA LVEAGLLALL SDVDALYEED 190 200 210 220 230 240 PKKNPQARPI PEVESVEAVL AHAGEENPLG SGGMKSKLLA ARIAGRVGIP TLLLPGKRPG 250 260 270 280 290 300 VLLQALSGAP LGTYFHARRR YRGEKAWLFG LLRPKGELVL DRGAVRALKE RGASLLPAGV 310 320 330 340 350 360 KEVRGRFSRG EAVRLLSEEG EEVGVGLANY ASEEIARIKG RRSAEIEAVL GYRYTEEVVH 370 RDHLALKEEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequence analysis of the proBA operon from an extremely thermophilic eubacterium Thermus thermophilus." Kosuge T., Tabata K., Hoshino T. FEMS Microbiol. Lett. 123:55-61(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of the extreme thermophile Thermus thermophilus." Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J. Nat. Biotechnol. 22:547-553(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB27 / ATCC BAA-163 / DSM 7039.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D29973 Genomic DNA. Translation: BAA06237.1. AE017221 Genomic DNA. Translation: AAS81905.1.
RefSeq	YP_005532.1. NC_005835.1.
3D structure databases
ProteinModelPortal	Q60050.
ModBase	Search...
Protein-protein interaction databases
STRING	262724.TTC1563.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAS81905; AAS81905; TT_C1563.
GeneID	2776015.
KEGG	tth:TTC1563.
PATRIC	23953563. VBITheThe54392_1559.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0263.
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_THET2

Accession

Primary (citable) accession number: Q60050

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 24, 2004
Last modified:	May 1, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program