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 Q87S07

Entry ID Method Resolution Chain Position Source
AF-Q87S07-F1 Predicted AlphaFoldDB

No variants for Q87S07

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q87S07

No associated diseases with Q87S07

2 regional properties for Q87S07

Type Name Position InterPro Accession
domain IMP dehydrogenase/GMP reductase 8 - 317 IPR001093
conserved_site IMP dehydrogenase / GMP reductase, conserved site 166 - 178 IPR015875

Functions

Description
EC Number 6.3.5.2 Carbon--nitrogen ligases with glutamine as amido-N-donor
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.
GMP synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: ATP + XMP + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate + 2H(+).
pyrophosphatase activity Catalysis of the hydrolysis of a pyrophosphate bond (diphosphate bond) between two phosphate groups.

1 GO annotations of biological process

Name Definition
glutamine metabolic process The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTKNIHDQRI LILDFGSQYT QLVARRVREI GVYCELWSWD VEEADIREFN PDGIILSGGP
70 80 90 100 110 120
ESVTEENSPR APQYVFDSGV PVLGVCYGMQ TMAEQLGGKV AGSNEREFGY AQVKVSGESA
130 140 150 160 170 180
IFKDLEATQD VWMSHGDKVV EIPADFVKVG ETDTCPYAAM ANEEKKYYGV QFHPEVTHTK
190 200 210 220 230 240
GGLQMLENFV LGVCGCERLW TSESIIEDAV ARIKEQVGDD EVILGLSGGV DSSVVAMLVH
250 260 270 280 290 300
RAIGDKLTCV FVDNGLLRLN EGQQVMDMFG DKFGLNIIKV DAEERFLEAL KGKSDPEEKR
310 320 330 340 350 360
KTIGHVFVDV FDEESKKLKN AKWLAQGTIY PDVIESAASK TGKAHVIKSH HNVGGLPDDM
370 380 390 400 410 420
EMGLVEPLRE LFKDEVRKIG LELGLPYNML YRHPFPGPGL GVRVLGEIKK EYCDLLRRAD
430 440 450 460 470 480
AIFIEELHAA DLYDKVSQAF TVFLPVRSVG VMGDGRKYDW VVSLRAVETI DFMTAHWAHL
490 500 510
PYDFLGKVSN RIINEVEGIS RVVYDISGKP PATIEWE