B2HIH4 (SYE_MYCMM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS

Gene names

Name:	gltX
Ordered Locus Names:	MMAR_1719

Organism

Mycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP]

Taxonomic identifier

216594 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	489 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP MF_00022_B
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B
Subunit structure	Monomer By similarity. HAMAP MF_00022_B
Subcellular location	Cytoplasm By similarity HAMAP MF_00022_B.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 489	489	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_0000367715
Regions
	Motif	12 – 22	11	"HIGH" region HAMAP MF_00022_B
	Motif	256 – 260	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	259	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	B2HIH4 [UniParc]. Last modified June 10, 2008. Version 1. Checksum: 94C9207AEFE1FC89	FASTA	489	53,715
	10 20 30 40 50 60 MTSSSVRVRF CPSPTGIPHV GMVRTALFNW AYARHTGGTF VFRIEDTDAA RDSEESYLAL 70 80 90 100 110 120 LDALRWLGLD WDEGPEVDGP YGPYRQSQRT EIYHDVVAKL LTAGEAYYAF STPEEVEARH 130 140 150 160 170 180 IAAGRNPKLG YDNFDRQLTD SQRAAYLAEG RKPVVRLRMP DTDLAWHDLV RGPTTFAAGS 190 200 210 220 230 240 VPDFALTRAT GDPLYTLVNP CDDALMKITH VLRGEDLLPS TPRQIALYQA LMRIGIAERV 250 260 270 280 290 300 PEFAHLPTVL GEGTKKLSKR DPQSNLFAHR DRGFIPEGLL NYLALLGWAI ADDHDLFSLD 310 320 330 340 350 360 EMVAAFDVAD VNSNPARFDQ KKADAINAEH IRMLDVADFT ARLRAYLDTH GHQLALDDAA 370 380 390 400 410 420 FAVAAELVQT RIVVLEDAWA LLKFLNDDRY AIDPKAAAKE LGPDAGPVLD AAIAALDGAA 430 440 450 460 470 480 DWTTADIEAA LKTALIEGMA LKPRKAFGPI RVAATGTTVS PPLFESLELL GRERSLGRLR SARDQVGSP

References

[1]

"Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis." Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. , Mungall K., Norbertczak H., Quail M.A., Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T. Genome Res. 18:729-741(2008) [PubMed: 18403782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-535 / M.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000854 Genomic DNA. Translation: ACC40168.1.
RefSeq	YP_001850023.1. NC_010612.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	B2HIH4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000031506; EBMYCP00000029946; EBMYCG00000031501.
GeneID	6225976.
GenomeReviews	Gene locus MMAR_1719 in contig CP000854_GR.
KEGG	mmi:MMAR_1719.
PATRIC	18064305. VBIMycMar75906_1839.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000016746.
HOGENOM	HBG628189.
OMA	AYEVYAY.
ProtClustDB	PRK01406.
Family and domain databases
HAMAP	MF_00022_B. Glu_tRNA_synth_B. [Tree]
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR004527. Glu-tRNA-synth_Ib_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ib. IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KO	K01885.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 1 hit. PTHR10119:SF1. PTHR10119:SF1. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
SUPFAM	SSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMs	TIGR00464. GltX_bact. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE_MYCMM

Accession

Primary (citable) accession number: B2HIH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	June 10, 2008
Last modified:	January 25, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program