Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for A8APT2

Entry ID Method Resolution Chain Position Source
AF-A8APT2-F1 Predicted AlphaFoldDB

No variants for A8APT2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8APT2

No associated diseases with A8APT2

4 regional properties for A8APT2

Type Name Position InterPro Accession
domain Glutamate-ammonia ligase adenylyltransferase, repeated domain 31 - 273 IPR005190-1
domain Glutamate-ammonia ligase adenylyltransferase, repeated domain 553 - 805 IPR005190-2
domain PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase 297 - 436 IPR013546-1
domain PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase 825 - 916 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
MKPLSSPLQQ HWQTVVERLP EILAEATLSV QAKSVLTFSD FVQDSVIAHP EWLTELESAP
70 80 90 100 110 120
PQADEWRHYA AWLQDALAQV TDEAALMREL RVFRRRIMVR IAWAQALSLV EEENILQQLS
130 140 150 160 170 180
HLAETLIVAA RDWLYDACCR EWGTPCNHDG VPQPLLILGM GKLGGGELNF SSDIDLIFAW
190 200 210 220 230 240
PEHGSTRGGR RELDNAQFFT RMGQRLIKVL DQPTMDGFVY RVDMRLRPFG DSGPLVLSFA
250 260 270 280 290 300
ALEDYYQEQG RDWERYAMVK ARIMGAADSA YVDELRAMLR PFVFRRYIDF SVIQSLRNMK
310 320 330 340 350 360
GMIAREVRRR GLKDNIKLGA GGIREIEFIV QVFQLIRGGR EPSLQSRSLL PTLSAIDALH
370 380 390 400 410 420
LLPENDAGQL RAAYLFLRRL ENLLQSINDE QTQTLPGDEL NRARLAWGMR TDDWSQLTDI
430 440 450 460 470 480
LAAHMANVRR VFNELIGDDE TDTQEDTLSE HWRELWQDAL QEDDTTPVLA HLSDDDRGRV
490 500 510 520 530 540
LALIADFRKE LDKRTIGPRG RQVLDHLMPH LLSDVCSRED ASVPLSRITP LLVGIVTRTT
550 560 570 580 590 600
YLELLSEFPG ALKHLISLCA ASPMVASQLA RYPLLLDELL DPNTLYQPTA TDAYRDELRQ
610 620 630 640 650 660
YLLRVPEDDE EQQLEALRQF KQTQLLRIAA ADIAGTLPVM KVSDHLTWLA EAIIDAVVQQ
670 680 690 700 710 720
AWGQMVARYG QPTHLAERTG RGFAVVGYGK LGGWELGYSS DLDLIFLHDC PMDVMTDGER
730 740 750 760 770 780
EIDGRQFYLR LAQRIMHLFS TRTSSGILYE VDARLRPSGA AGMLVTSAEA FADYQKNEAW
790 800 810 820 830 840
TWEHQALVRA RVVYGDPQLT SQFDAVRRDI MTLAREGKTL QTEVREMREK MRAHLGNKHR
850 860 870 880 890 900
DRFDIKADEG GITDIEFITQ YLVLRYAHEK PKLTRWSDNV RILELLAQND IMDEQEAHAL
910 920 930 940
TLAYTTLRDE LHHLALQELP GHVAQECFSK ERALVRASWQ KWLVAG