Q58772

PR
Gene name
gltX
Protein name
Glutamate--tRNA ligase
Names
Glutamyl-tRNA synthetase, GluRS
Species
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
KEGG Pathway
mja:MJ_1377
EC number
6.1.1.17: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

10-114 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q58772

Entry ID Method Resolution Chain Position Source
AF-Q58772-F1 Predicted AlphaFoldDB

No variants for Q58772

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q58772

No associated diseases with Q58772

4 regional properties for Q58772

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 11 - 22 IPR001412
domain Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain 6 - 321 IPR020058
domain Glutamyl-tRNA synthetase 4 - 329 IPR033910
domain Aminoacyl-tRNA synthetase, class I, anticodon-binding 355 - 481 IPR045462

Functions

Description
EC Number 6.1.1.17 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
glutamate-tRNA ligase activity Catalysis of the reaction: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).

2 GO annotations of biological process

Name Definition
amide biosynthetic process The chemical reactions and pathways resulting in the formation of an amide, any derivative of an oxoacid in which an acidic hydroxy group has been replaced by an amino or substituted amino group.
glutamyl-tRNA aminoacylation The process of coupling glutamate to glutamyl-tRNA, catalyzed by glutamyl-tRNA synthetase. The glutamyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a glutamic acid-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEEKILPIAL RNAIKYNGKA NPKAVLGIFL SENPEYRSKA KEVMPIVEKV VEEVNKLSLD
70 80 90 100 110 120
EIKKKLEELG EDVKKKEKKE KGLELPNVKD KVVMRFAPNP SGPLHIGHAR AAVLNDYFVK
130 140 150 160 170 180
KYGGKLILRL EDTDPKRVLP EAYDMIKEDL DWLGVKVDEV VIQSDRIELY YEYGRKLIEM
190 200 210 220 230 240
GHAYVCDCNP EEFRELRNKG VPCKCRDRAI EDNLELWEKM LNGELENVAV RLKTDIKHKN
250 260 270 280 290 300
PSIRDFPIFR VEKTPHPRTG DKYCVYPLMN FSVPVDDHLL GMTHVLRGKD HIVNTEKQAY
310 320 330 340 350 360
IYKYFGWEMP EFIHYGILKI EDIVLSTSSM YKGIKEGLYS GWDDVRLGTL RALRRRGIKP
370 380 390 400 410 420
EAIYEIMKRI GIKQADVKFS WENLYAINKE LIDKDARRFF FVWNPKKLII EGAEKKVLKL
430 440 450 460 470 480
RMHPDRPEFG ERELIFDGEV YVVGDELEEN KMYRLMELFN IVVEKVDDIA LAKYHSDDFK
490 500 510 520 530 540
IARKNKAKII HWIPVKDSVK VKVLMPDGEI KEGFAEKDFA KVEVDDIIQF ERFGFVRIDK
550
KDNDGFVCCY AHR