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 Q8E1B0

Entry ID Method Resolution Chain Position Source
AF-Q8E1B0-F1 Predicted AlphaFoldDB

No variants for Q8E1B0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8E1B0

No associated diseases with Q8E1B0

1 regional properties for Q8E1B0

Type Name Position InterPro Accession
domain NADPH-dependent FMN reductase-like 36 - 179 IPR005025

Functions

Description
EC Number 6.3.1.1 Acid--ammonia (or amine) ligases (amide synthases)
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
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
aspartate-ammonia ligase activity Catalysis of the reaction: ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

1 GO annotations of biological process

Name Definition
L-asparagine biosynthetic process The chemical reactions and pathways resulting in the formation of asparagine, (2S)-2-amino-3-carbamoylpropanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKKSFIHQQQ EISFVKNTFT QYLIDKLEIV EVQGPILSQV GDGMQDNLSG IEHPVSVKVL
70 80 90 100 110 120
NIPEAEFEVV HSLAKWKRHT LARFGFNEGE GLFVHMKALR PDEDSLDPTH SVYVDQWDWE
130 140 150 160 170 180
KVIPDGRRNL DYLKETVEKI YKAIRLTELA VEARFDIESI LPKRITFIHT EELVEKYPDL
190 200 210 220 230 240
SPKERENAIA KEYGAVFLIG IGGELADGKP HDGRAPDYDD WTTPSENGFK GLNGDILVWN
250 260 270 280 290 300
EQLGTAFELS SMGIRVDEDA LKRQVVLTGD EDRLEFEWHK TLLRGFFPLT IGGGIGQSRL
310 320
AMFLLRKKHI GEVQSSVWPK EVRDTFENIL