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 A0R2Y2

Entry ID Method Resolution Chain Position Source
AF-A0R2Y2-F1 Predicted AlphaFoldDB

No variants for A0R2Y2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A0R2Y2

No associated diseases with A0R2Y2

2 regional properties for A0R2Y2

Type Name Position InterPro Accession
domain ATP-grasp fold, ATP-dependent carboxylate-amine ligase-type 124 - 301 IPR003135
domain ATP-grasp fold 120 - 315 IPR011761

Functions

Description
EC Number 6.3.1.21 Acid--ammonia (or amine) ligases (amide 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

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ligase activity Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient.
magnesium ion binding Binding to a magnesium (Mg) ion.
phosphoribosylglycinamide formyltransferase 2 activity Catalysis of the reaction: formate + ATP + 5'-phospho-ribosylglycinamide = 5'-phosphoribosyl-N-formylglycinamide + ADP + diphosphate.
phosphoribosylglycinamide formyltransferase activity Catalysis of the reaction: 10-formyltetrahydrofolate + N1-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide.

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
MTTIGTPLSP RATKVMLLGS GELGREVLIA LQRLGVETIA VDRYENAPGH QVAHHARTIA
70 80 90 100 110 120
MSDPDQLRAL IEAERPDLVV PEIEAIATPV LEALEAEGVT TVIPTARATR LTMDREGIRR
130 140 150 160 170 180
LAAETLGVPT SPYRFCDSLA ELQAAIDDEI GYPCVVKPVM SSSGKGQSKI NGPDEVAAAW
190 200 210 220 230 240
EYAMAGGRVS HTRIIVEGFV DFDYEITLLT VRARGADGEI ATQFCEPIGH RQVGGDYVES
250 260 270 280 290 300
WQPHPMPATA LERAQEIAGA VTGNLGGQGI FGVELFVKGD QVWFSEVSPR PHDTGMVTMV
310 320 330 340 350 360
TQWQNEFELH ARAILGLPVD TTLRAPGASA VIYGGVDATG VVFDGVDAAL QVPHTDIRLF
370 380 390
GKPESFVKRR MGVALAFDDD VQTARRNAAE AASRMKPRAV