Q7TUT1 (GLUQ_PROMM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamyl-Q tRNA(Asp) synthetase
Short name=Glu-Q-RSs
EC=6.1.1.-

Gene names

Name:	gluQ
Ordered Locus Names:	PMT_1394

Organism

Prochlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]

Taxonomic identifier

74547 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	306 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon By similarity. HAMAP MF_01428
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_01428
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily.

Ontologies

Keywords
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	tRNA aminoacylation for protein translation Inferred from electronic annotation. Source: InterPro tRNA modification Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW aminoacyl-tRNA ligase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 306	306	Glutamyl-Q tRNA(Asp) synthetase HAMAP MF_01428		PRO_0000208312
Regions
	Region	29 – 33	5	Glutamate binding By similarity
	Motif	32 – 42	11	"HIGH" region HAMAP MF_01428
	Motif	244 – 248	5	"KMSKS" region HAMAP MF_01428
Sites
	Metal binding	121	1	Zinc By similarity
	Metal binding	123	1	Zinc By similarity
	Metal binding	141	1	Zinc By similarity
	Metal binding	145	1	Zinc By similarity
	Binding site	65	1	Glutamate By similarity
	Binding site	188	1	Glutamate By similarity
	Binding site	206	1	Glutamate By similarity
	Binding site	247	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7TUT1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 474CFA6E2DA1BE10	FASTA	306	34,097
	10 20 30 40 50 60 MAKSSALPDH LYEQMEVGQR LRNQGYRGRF APSPTGPLHL GNLCTALVSW LQARLANGAW 70 80 90 100 110 120 LLRVDDLDQP RNRVGAVESL QQDLHWLGLE WDGPVVFQSR RRGIYNSFLS ALRRQGKLYA 130 140 150 160 170 180 CRCSRRMLAD ISAPAGRHLV YPGTCRDLEL FWGWHEGRLP SWRLRVSKEF SHTSGDVILR 190 200 210 220 230 240 RADGFIAYHL ATVVDELTLG ISEVVRGEDL LDAMNAQLAL INAISERPVI YRHVPLLCDD 250 260 270 280 290 300 QGRKLAKREG HAGLDSLRSE GLGPSHVVGW LAASQSLVPF GAELTAGELL SELKKKEGVL KSVLKP

References

[1]

"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation." Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W. Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MIT 9313.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX548175 Genomic DNA. Translation: CAE21569.1.
RefSeq	NP_895221.1. NC_005071.1.
3D structure databases
ProteinModelPortal	Q7TUT1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7TUT1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1728615.
GenomeReviews	Gene locus PMT_1394 in contig BX548175_GR.
KEGG	pmt:PMT1394.
NMPDR	fig|74547.1.peg.1388.
PATRIC	23011289. VBIProMar135351_1790.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	DAPSSYH.
PhylomeDB	Q7TUT1.
ProtClustDB	PRK05710.
Enzyme and pathway databases
BioCyc	PMAR74547:PMT1394-MONOMER.
Family and domain databases
HAMAP	MF_01428. Glu_Q_tRNA_synth. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR022380. Glu-Q_TRNA(Asp)_Synthase. IPR000924. Glu/Gln-tRNA-synth_Ib. IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KO	K01885.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 2 hits. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLUQ_PROMM

Accession

Primary (citable) accession number: Q7TUT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program