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 A6TE32

Entry ID Method Resolution Chain Position Source
AF-A6TE32-F1 Predicted AlphaFoldDB

No variants for A6TE32

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6TE32

No associated diseases with A6TE32

4 regional properties for A6TE32

Type Name Position InterPro Accession
domain Glutamate-ammonia ligase adenylyltransferase, repeated domain 31 - 275 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 - 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
MMPLSPQLQQ HWQTVADRLP ADFPVAELSP QARSVMAFSD FVEQSVIAQP GWLNELADSA
70 80 90 100 110 120
PAAEEWRHYE AWLQERLQAV TDEAGLMREL RLFRRQMMVR IAWAQALSLV REEETLQQLS
130 140 150 160 170 180
VLAETLIVAA RDWLYAACCK EWGTPCNAEG QPQPLLILGM GKLGGGELNF SSDIDLIFAW
190 200 210 220 230 240
PEHGATRGGR RELDNAQFFT RLGQRLIKAL DQPTQDGFVY RVDMRLRPFG DSGPLVLSFA
250 260 270 280 290 300
ALEDYYQEQG RDWERYAMVK ARIMGDNDGA YASELRAMLR PFVFRRYIDF SVIQSLRNMK
310 320 330 340 350 360
GMIAREVRRR GLKDNIKLGA GGIREIEFIV QVFQLIRGGR EPALQQRALL PTLAAIDELH
370 380 390 400 410 420
LLPEGDATLL RAAYLFLRRL ENLLQSINDE QTQTLPQDEL NRARLAWGMH TDDWETLSAQ
430 440 450 460 470 480
LANHMANVRR VFNELIGDDE AQSPDEQLAE YWRELWQDAL EEDDASPALA HLNDADRRSV
490 500 510 520 530 540
LALIADFRKE LDRRTIGPRG RQVLDQLMPH LLSEICSRAD APLPLARITP LLTGIVTRTT
550 560 570 580 590 600
YLELLSEFPG ALKHLITLCA ASPMVASQLA RHPLLLDELL DPNTLYQPTA TDAYRDELRQ
610 620 630 640 650 660
YLLRVPEEDE EQQLEALRQF KQAQQLHIAA ADIAGTLPVM KVSDHLTWLA EAILDAVVQQ
670 680 690 700 710 720
AWGQMVARYG LPTHLHDRQG RGFAVVGYGK LGGWELGYSS DLDLVFLHDC PAEVMTDGER
730 740 750 760 770 780
EIDGRQFYLR LAQRIMHLFS TRTSSGILYE VDARLRPSGA AGMLVTTADA FADYQQNEAW
790 800 810 820 830 840
TWEHQALVRA RVVYGDPALQ ARFDAIRRDI LTTPREGATL QTEVREMREK MRAHLGNKHP
850 860 870 880 890 900
NRFDIKADAG GITDIEFITQ YLVLRYASDK PKLTRWSDNV RILELLAQND IMDEEEARAL
910 920 930 940
THAYTTLRDA LHHLALQELP GHVAPEAFSR EREQVSASWQ KWLMA