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 B0RMY6

Entry ID Method Resolution Chain Position Source
AF-B0RMY6-F1 Predicted AlphaFoldDB

No variants for B0RMY6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0RMY6

No associated diseases with B0RMY6

3 regional properties for B0RMY6

Type Name Position InterPro Accession
conserved_site SAICAR synthetase, conserved site 119 - 133 IPR018236-1
conserved_site SAICAR synthetase, conserved site 218 - 226 IPR018236-2
domain SAICAR synthetase/ADE2, N-terminal 15 - 306 IPR028923

Functions

Description
EC Number 6.3.2.6 Acid--amino-acid ligases (peptide synthases)
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

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
phosphoribosylaminoimidazolesuccinocarboxamide synthase activity Catalysis of the reaction: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate + ATP = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate.

1 GO annotations of biological process

Name Definition
'de novo' IMP biosynthetic process The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPVSTTLLQS DLPGLPLRHR GKVRDVFDIP RDRLPADAPP GDYLLMVATD RLSAFDVVLP
70 80 90 100 110 120
DPIPGKGEML CQVSNFWFHK TEHLMPNHLV DIRVEQVLPE GVDPALYAKR AVVTRKLKPV
130 140 150 160 170 180
PVEAIARGYL IGSGWKDYQR TGKISGIELP DGLRQAEKLP EPIFTPSTKA AVGDHDENID
190 200 210 220 230 240
FDAMVKTVGA ELAERVRDAT LRIYRFAADF AAERGILLAD TKFEFGTDAD GRLYIMDEML
250 260 270 280 290 300
TPDSSRYWPA DQYELGTSPP SYDKQFVRDY LETLDWGKTA PGPRLPADVI ERTRAKYAEA
LQRLAGISVD