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 A6U1F7

Entry ID Method Resolution Chain Position Source
AF-A6U1F7-F1 Predicted AlphaFoldDB

No variants for A6U1F7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6U1F7

No associated diseases with A6U1F7

2 regional properties for A6U1F7

Type Name Position InterPro Accession
domain IMP dehydrogenase/GMP reductase 4 - 316 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
MKIFDYEDIQ LIPNKCIVES RSECDTTIQF GPKKFKLPVV PANMQTVMNE KLAKWFAEND
70 80 90 100 110 120
YFYIMHRFDE EARIPFIKHM QNSGLFASIS VGVKKAEFDF IEKLAQEKLI PEYITIDIAH
130 140 150 160 170 180
GHSDSVINMI KHIKNHIPDS FVIAGNVGTP EGVRELENAG ADATKVGIGP GRVCITKIKT
190 200 210 220 230 240
GFGTGGWQLA ALNICSKAAR KPLIADGGIR THGDIAKSIR FGASMVMIGS LFAAHEESPG
250 260 270 280 290 300
ETVELDGKQY KEYFGSASEF QKGEHKNVEG KKMFVEHKGS LMDTLKEMQQ DLQSSISYAG
310 320
GKDLKSLRTV DYVIVRNSIF NGDRD