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 B2USX4

Entry ID Method Resolution Chain Position Source
AF-B2USX4-F1 Predicted AlphaFoldDB

No variants for B2USX4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2USX4

No associated diseases with B2USX4

2 regional properties for B2USX4

Type Name Position InterPro Accession
domain IMP dehydrogenase/GMP reductase 4 - 315 IPR001093
conserved_site IMP dehydrogenase / GMP reductase, conserved site 164 - 176 IPR015875

Functions

Description
EC Number 1.7.1.7 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
GMP reductase complex An oxidoreductase complex which is capable of GMP reductase activity. It catalyses the irreversible reaction: GMP + 2 H(+) + NADPH => IMP + NADP(+) + NH(4)(+).

1 GO annotations of molecular function

Name Definition
GMP reductase activity Catalysis of the reaction: IMP + NADP(+) + NH(4)(+) = GMP + 2 H(+) + NADPH.

1 GO annotations of biological process

Name Definition
purine nucleotide metabolic process The chemical reactions and pathways involving a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKIFDYENIQ LIPNKCIVNS RSECDTTVTL GRHTFKMPIV PANMQTIIND SIAEFLAENG
70 80 90 100 110 120
YFYIMHRFDG AARIPFVKKM KERQWISSIS VGVKKEEYLF IEELAKQKLA SDYITIDIAH
130 140 150 160 170 180
GHSNSVIEMI QHIKTHLPET FVIAGNVGTP EAVRELENAG ADATKVGIGP GKACITKIKT
190 200 210 220 230 240
GFGTGGWQLA ALRWCAKAAR KPIIADGGIR THGDIAKSIR FGATMVMIGS LFAGHEESSG
250 260 270 280 290 300
ETKIENGIAY KEYFGSASEF QKGEKKNIEG KKIWIQHKGS LKDTLIEMHQ DLQSSISYAG
310 320
GRDLEAIRKV DYVIVKNSIF NGDAI