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 Q8KCW4

Entry ID Method Resolution Chain Position Source
AF-Q8KCW4-F1 Predicted AlphaFoldDB

No variants for Q8KCW4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8KCW4

No associated diseases with Q8KCW4

2 regional properties for Q8KCW4

Type Name Position InterPro Accession
domain IMP dehydrogenase/GMP reductase 6 - 317 IPR001093
conserved_site IMP dehydrogenase / GMP reductase, conserved site 166 - 178 IPR015875

Functions

Description
EC Number 1.1.1.205 With NAD(+) or NADP(+) as acceptor
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
IMP dehydrogenase activity Catalysis of the reaction: inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH + H+.
metal ion binding Binding to a metal ion.
nucleotide binding Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.

1 GO annotations of biological process

Name Definition
GMP biosynthetic process The chemical reactions and pathways resulting in the formation of GMP, guanosine monophosphate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDKILYDALT FDDVLLVPAY SNVLPKETVV KSRLTRQIEV NIPLVSAAMD TVTEAELAIA
70 80 90 100 110 120
LARAGGIGII HKNLSIDEQA RQVAKVKRFE SGIIRNPIHL FEDATIQDAI DLMIRHSISG
130 140 150 160 170 180
IPVVEHPTPE GCLLLKGIVT NRDLRMTASS DEKITTIMTT NLVTAKEGID LLTAEDILMR
190 200 210 220 230 240
NKIEKLLIID DNGYLKGLIT FKDIQKRKQC PDACKDSQGR LRAGAAVGIR ANTMSRVDAL
250 260 270 280 290 300
VAAGVDVVAV DTAHGHSQAV LDMVATIKQK YPELQVIAGN VATPEAVRDL VKAGADAVKV
310 320 330 340 350 360
GIGPGSICTT RIVAGVGMPQ LTAIMKCAEE AKKTDIPLIA DGGIKYSGDI AKALAAGADS
370 380 390 400 410 420
VMMGSVFAGT DESPGETILY EGRRFKAYRG MGSLGAMSEP EGSSDRYFQD VSAETKKYVP
430 440 450 460 470 480
EGIEGRIPAK GKLDEVVYQL IGGLKSAMGY CGVRTITELK ENTRFVRITS AGLRESHPHD
490
VMITKEAPNY STSA