Q8ZU33

PR
Gene name
gltX
Protein name
Glutamate--tRNA ligase
Names
Glutamyl-tRNA synthetase, GluRS
Species
Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)
KEGG Pathway
pai:PAE2969
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)

5-119 (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 Q8ZU33

Entry ID Method Resolution Chain Position Source
AF-Q8ZU33-F1 Predicted AlphaFoldDB

No variants for Q8ZU33

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8ZU33

No associated diseases with Q8ZU33

4 regional properties for Q8ZU33

Type Name Position InterPro Accession
domain Glutamate-ammonia ligase adenylyltransferase, repeated domain 13 - 251 IPR005190-1
domain Glutamate-ammonia ligase adenylyltransferase, repeated domain 517 - 770 IPR005190-2
domain PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase 279 - 418 IPR013546-1
domain PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase 793 - 888 IPR013546-2

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and pathways resulting in the formation of an amide, any derivative of an oxoacid in which an acidic hydroxy group has been replaced by an amino or substituted amino group.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
MNVEEIAFKY ALANAVKYGG KADVKAVMAK LMAEVPELRA RAREVKQIVD AVVARVNSMP
70 80 90 100 110 120
LEEQRRILRE RWPELLEERR AEQRRPGLEG LPELPNVRGG VVVRFAPNPD FVLHLGSARP
130 140 150 160 170 180
AILNYAYRIK YGGKFILRFE DTDPRIKSPL VTEEVNAYES IREDLRWLGV RWDEEYIQSQ
190 200 210 220 230 240
RMEIYYEHAK KLLEMGAAYV DLCKPEEWRR LRNEKKACPH REQPPEVNLE LWDKMLEGRF
250 260 270 280 290 300
KEGEAVLRIK TDLTHPDPSV RDWVAFRIID TSKTPHPLTG DKYIVWPTYN FAVSIDDHLM
310 320 330 340 350 360
GVTHVLRAQE HSVNTIKQSY VFRHFGWEQP VTIHFGRLRI EGATLSKSKL KAMRIKYDDL
370 380 390 400 410 420
TLPTLAGLRN RGIVPEAIWD LILSVGIKPS DSTVALANLF AFNRKHIEPI ADRYMYVADP
430 440 450 460 470 480
VKLVFEADKE LTAHVPFHPS FKERGERTYR LGPGRVEVYI QRRDAVAGKV VRLMELANVE
490 500 510 520 530 540
IVRVEGDVAY GRIHSYSLDE AKKIGAPIIQ WVWDPVEITV IKPAGVGRKE VEVGLGEGWL
550 560
ERVEVGKYVQ FFRYGYLKKR GPREFVFLHD