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 P91134

Entry ID Method Resolution Chain Position Source
AF-P91134-F1 Predicted AlphaFoldDB

No variants for P91134

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P91134

No associated diseases with P91134

2 regional properties for P91134

Type Name Position InterPro Accession
binding_site Adenylosuccinate synthase, GTP-binding site 38 - 45 IPR018220
active_site Adenylosuccinate synthase, active site 164 - 175 IPR033128

Functions

Description
EC Number 6.3.4.4 Other carbon--nitrogen ligases
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.

3 GO annotations of molecular function

Name Definition
adenylosuccinate synthase activity Catalysis of the reaction: L-aspartate + GTP + IMP = N(6)-(1,2-dicarboxyethyl)-AMP + GDP + 3 H(+) + phosphate.
GTP binding Binding to GTP, guanosine triphosphate.
magnesium ion binding Binding to a magnesium (Mg) ion.

2 GO annotations of biological process

Name Definition
'de novo' AMP biosynthetic process The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from inosine 5'-monophosphate (IMP).
IMP metabolic process The chemical reactions and pathways involving IMP, inosine monophosphate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGSVTSKTND ELESFLNKRL GGSMTSSNKT VSVLLGAQWG DEGKGKIIDY LIENHKINVT
70 80 90 100 110 120
ARCQGGNNAG HTVVANGRKY DFHILPSGII SPTCFNVIGN GVVVNLDAFF SELAHNGILE
130 140 150 160 170 180
ESGWEKRIMI SSEAHLVFGV HSQVDGRQED SLAAKNKIGT TNRGIGPTYS SKCFRNGIRV
190 200 210 220 230 240
ADLMADFEEF SEKYRRLVEH YKKQFPSIEV NVDEELAKFK QHREKLAELK LVGDTVGFIH
250 260 270 280 290 300
EQRNAGKQVL VEGANGALLD IDFGTYPYVT SSNSTVGGAC TGIGVPPTAV GNVIGVVKAY
310 320 330 340 350 360
QTRVGTGPFP TELFDSDGEK LQTIGKEVGV TTGRKRRCGW IDLFLLRRSA MINGYTAIAL
370 380 390 400 410 420
TKLDILDTFP TIKVAVGYKL NGQVLSSPPA QANAWGAIEV EYKEFEGWNE PTVGVRKFED
430 440 450
LPEKCRQYVK FIEDFIKVPI VYIGVGAERE SLIVRQQ