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 B1L3X7

Entry ID Method Resolution Chain Position Source
AF-B1L3X7-F1 Predicted AlphaFoldDB

No variants for B1L3X7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B1L3X7

No associated diseases with B1L3X7

3 regional properties for B1L3X7

Type Name Position InterPro Accession
domain IMP biosynthesis enzyme PurP, C-terminal 176 - 365 IPR009720
domain IMP biosynthesis enzyme PurP, N-terminal 21 - 145 IPR010672
domain ATP-grasp fold 131 - 357 IPR011761

Functions

Description
EC Number 6.3.4.23 Other carbon--nitrogen ligases
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

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ligase activity, forming carbon-nitrogen bonds Catalysis of the joining of two molecules, or two groups within a single molecule, via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate.
magnesium ion binding Binding to a magnesium (Mg) ion.

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
MIPRERILSV LSKYDESDVK IGTICSHSSL QIFNGARREG LRSVGIVLRE NKPYYESFPR
70 80 90 100 110 120
ASPDIFIEVD SYGDLLSEET QEELISENVI MIPHGSFVEY VGSENILERF RVPMFGNRLT
130 140 150 160 170 180
LYWEGDRRRQ RKWLEDAGVP TPRIYRSPED IDRPVIVKLH GAKGGKGYFK ASSPEEFYEK
190 200 210 220 230 240
FSELKERGLV GSLEDVVIEE FIVGVRFYPH FFFSPIEGEN IADLEGGRLE LLGIDRRLEV
250 260 270 280 290 300
IDEIHRGLPD LMEDFMDYTV TGNIPVIVRE KYLVDLLRDA VKIISSSRRL FYPGLIGPFC
310 320 330 340 350 360
MEMIYNPSRG FITFEVSARI VAGTNLYTDG SPYSYYYYDE PMSMGRRIAR EIKEAVKSGS
LHKIIY