A9MPW2

PR
Gene name
glnE
Protein name
Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
Names
ATP:glutamine synthetase adenylyltransferase, ATase
Species
Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)
KEGG Pathway
ses:SARI_04428
EC number
2.7.7.42: Nucleotidyltransferases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

411-540 (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 A9MPW2

Entry ID Method Resolution Chain Position Source
AF-A9MPW2-F1 Predicted AlphaFoldDB

No variants for A9MPW2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A9MPW2

No associated diseases with A9MPW2

4 regional properties for A9MPW2

Type Name Position InterPro Accession
domain Glutamate-ammonia ligase adenylyltransferase, repeated domain 31 - 274 IPR005190-1
domain Glutamate-ammonia ligase adenylyltransferase, repeated domain 554 - 806 IPR005190-2
domain PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase 297 - 436 IPR013546-1
domain PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase 826 - 917 IPR013546-2

Functions

Description
EC Number 2.7.7.42 Nucleotidyltransferases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

4 GO annotations of molecular function

Name Definition
[glutamate-ammonia-ligase] adenylyltransferase activity Catalysis of the reaction: ATP + [L-glutamate:ammonia ligase (ADP-forming)] = diphosphate + adenylyl-[L-glutamate:ammonia ligase (ADP-forming)].
[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase Catalysis of the reaction: adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O = AMP + [L-glutamate:ammonia ligase (ADP-forming)].
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
magnesium ion binding Binding to a magnesium (Mg) ion.

2 GO annotations of biological process

Name Definition
metabolic process The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation.
regulation of glutamine family amino acid metabolic process Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving amino acids of the glutamine family, comprising arginine, glutamate, glutamine and proline.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTPLSSPLRQ YWQTVVERLP EGFTETSLSA QAKSVLTFSD FALDSVIAHP EWLAELESAS
70 80 90 100 110 120
PQADEWRHYA GWLQEALADV CDDASLMREL RLFRRRIMVR IAWAQALSRV EDETILQQLS
130 140 150 160 170 180
HLAETLIVGA RDWLYAACCR EWGTPCNPQG VPQPLLILGM GKLGGGELNF SSDIDLIFAW
190 200 210 220 230 240
PEHGTTQGGR RELDNAQFFT RLGQRLIKAL DQPTMDGFVY RVDMRLRPFG DSGPLVLSFA
250 260 270 280 290 300
ALEDYYQEQG RDWERYAMVK ARIMGDNNDA WSRELRAMLR PFVFRRYIDF SVIQSLRNMK
310 320 330 340 350 360
GMIAREVRRR GLKDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL PTLNAITALH
370 380 390 400 410 420
LLPENDVTQL RAAYLFLRRL ENLLQSINDE QTQTLPADDL NRARLAWGMN TDNWPQLVGK
430 440 450 460 470 480
LTEHMANVRR VFNELIGDDE ADTPQEEELS EPWREVWQDT LQEGDSTPVL AHLADEDRRQ
490 500 510 520 530 540
LLTLIADFRK ELDKRPIGPR GRQVLDQLMP RLLDDVCSRE DAAVTLSRIT PLLAGIVTRT
550 560 570 580 590 600
TYLELLSEFP GALKHLIMLC AASPMIASQL ARYPLLLDEL LDPGTLYQPT ATNAYRDELR
610 620 630 640 650 660
QYLLRVPEED EEQQLEALRQ FKQAQLLRIA AADIAGTLSV MKVSDHLTWL AEAMIDAVVQ
670 680 690 700 710 720
QAWMQMVARY GQPTHLDERQ GRGFAVVGYG KLGGWELGYS SDLDLIFLHD CPIDVMTNGE
730 740 750 760 770 780
REIDGRQFYL RLAQRIMHLF STRTSSGILY EVDARLRPSG AAGMLVTSAD AFADYQQHEA
790 800 810 820 830 840
WTWEHQALVR ARVVYGDPQL TSQFDAVRRT IMTTARDGKT LQTEVREMRE KMRSHLGNKH
850 860 870 880 890 900
RDRFDIKADE GGITDIEFIA QYLVLRYAHE KPKLTRWSDN VRILELLAQN GIMDEHEAQA
910 920 930 940
LTVAYTTLRD ELHHLALQEL PGHVAQTCFS KERALVQASW RKWLVAV