A8GJU4

PR
Gene name
glnE
Protein name
Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
Names
ATP:glutamine synthetase adenylyltransferase, ATase
Species
Serratia proteamaculans (strain 568)
KEGG Pathway
spe:Spro_4290
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)

273-342 (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 A8GJU4

Entry ID Method Resolution Chain Position Source
AF-A8GJU4-F1 Predicted AlphaFoldDB

No variants for A8GJU4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8GJU4

No associated diseases with A8GJU4

4 regional properties for A8GJU4

Type Name Position InterPro Accession
domain Glutamate-ammonia ligase adenylyltransferase, repeated domain 36 - 277 IPR005190-1
domain Glutamate-ammonia ligase adenylyltransferase, repeated domain 554 - 805 IPR005190-2
domain PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase 298 - 437 IPR013546-1
domain PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase 826 - 918 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
MLPLSAALQT QAQNIVQRFQ ETQGADCALS SQELWVLASS DFVCDMLQSQ PEWLATLRKQ
70 80 90 100 110 120
PPVADEWQHY AAWLQDDLEE VRDEAQLMRA LRLFRRETLV RIAWAQALGQ CSTQETLLQL
130 140 150 160 170 180
SGLAETLIVS ARDWLYQTCC REWGTPCNAQ GVPQPLLILG MGKLGGGELN FSSDIDLIFA
190 200 210 220 230 240
YPENGQTQGG RRELDNAQFF TRLGQRLIKA LDQQTIDGFV YRVDMRLRPF GDSGPLVMSF
250 260 270 280 290 300
AALEDYYQEQ GRDWERYAMV KARLMGGSED AYSEELRKTL RPFVFRRYID FSVIQSLRNM
310 320 330 340 350 360
KGMIAREVRR RGLKDNIKLG AGGIREIEFI TQVFQLIRGG REPALQGRSL LPTLQAVGEL
370 380 390 400 410 420
GLLEPQQVQA MSASYLFLRR LENLLQAIAD QQTQTLPQDE LDQARLAWGM GFDDWSALLL
430 440 450 460 470 480
ALDHHMQAVR AVFNDLIGDD SPDVGEDPDY QHYHSLWQDA LEENELAPLT PHLDEEARRQ
490 500 510 520 530 540
MLRTIAEFRH DVDKRTIGPR GRDVLDQLMP RLLAEVCPRQ DAPTALLRLT QLLLSIVTRT
550 560 570 580 590 600
TYLELLVEYH AALSHLIRLC AASPMVANQL SRYPLLLDEL LEPATLYQPV APDAYRSELR
610 620 630 640 650 660
QYLLRVPEDD EEQRLEALRQ FKQAQQLRIA AGDISGALPV MKVSDHLTYL AEAIIDTVVQ
670 680 690 700 710 720
QAWNDMVARY GQPTHLQERE GRGFAVIGYG KLGGWELGYS SDLDLVFILD CPPEVMTDGD
730 740 750 760 770 780
RSIDGRQFYL RLAQRVMHLF STRTSSGILY EVDARLRPSG AAGMLVSTVE AFADYQQSEA
790 800 810 820 830 840
WTWEHQALVR ARIVHGDPLL HQQFDVIRRE ILCKPRDLET LKREVREMRE KMRNHLGNKQ
850 860 870 880 890 900
RELFDIKADE GGITDIEFIA QYLVLGYAAA EPRLTRWSDN VRIFELMANY DIMPEEEARA
910 920 930 940
LTQAYVTMRD EIHHLALQEH SGKIGNGQFA AEREQVRASW AKWLG