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 Q5N2F8

Entry ID Method Resolution Chain Position Source
AF-Q5N2F8-F1 Predicted AlphaFoldDB

No variants for Q5N2F8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5N2F8

No associated diseases with Q5N2F8

4 regional properties for Q5N2F8

Type Name Position InterPro Accession
domain GMP synthase, C-terminal 216 - 534 IPR001674
domain GMP synthase, glutamine amidotransferase 22 - 208 IPR004739
domain Glutamine amidotransferase 23 - 203 IPR017926
domain GMP synthetase ATP pyrophosphatase domain 211 - 409 IPR025777

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
MTLQTEMEAA LEVAALNREM LIILDFGSQY SELIARRIRE TQVYSEVLSY RTTADQIRQL
70 80 90 100 110 120
SPKGIILSGG PNSVYDDYAP VCDPEIWNLG IPVLGVCYGM QLMVQQLGGQ VDRAERGEYG
130 140 150 160 170 180
KAALVIDDPT DLLTNVEPGS TMWMSHGDSV KTMPEGFELL AHTDNTPCAA IADHQRKFYG
190 200 210 220 230 240
VQFHPEVVHS VHGMALIRNF VYHICDCEPT WTTETFVEEA IREIRARVGD KRVLLALSGG
250 260 270 280 290 300
VDSSTLAFLL HRAIGDQLTC MFIDQGFMRK GEPERLMEVF NEKFKIHVEY IQARDRFLQR
310 320 330 340 350 360
LEGITDPEEK RKRIGHEFIR VFEEESRRLG PFDYLAQGTL YPDVIESADT NVDPKTGERV
370 380 390 400 410 420
AVKIKSHHNV GGLPKDLQFK LVEPLRRLFK DEVRQVGRSL GLPEEIVKRH PFPGPGLAIR
430 440 450 460 470 480
ILGEVTAEKL NILRDADLIV RQEVNRQGYY DEFWQAFAVL LPVKSVGVMG DKRTYAYPVV
490 500 510 520 530
LRFVSSEDGM TADWSRAPYD LLETISNRIV NEVKGVNRVV YDITSKPPGT IEWE