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 Q2RGP2

Entry ID Method Resolution Chain Position Source
AF-Q2RGP2-F1 Predicted AlphaFoldDB

No variants for Q2RGP2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2RGP2

No associated diseases with Q2RGP2

4 regional properties for Q2RGP2

Type Name Position InterPro Accession
domain GMP synthase, C-terminal 207 - 516 IPR001674
domain GMP synthase, glutamine amidotransferase 12 - 198 IPR004739
domain Glutamine amidotransferase 14 - 194 IPR017926
domain GMP synthetase ATP pyrophosphatase domain 202 - 391 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
MIGENKQLAE IVLVLDFGGQ YNQLIARRVR EAGVYSEMIP YNTPLEKILA RRPRGIIFSG
70 80 90 100 110 120
GPASVYSLGA PRIDRALYES GIPILGICYG MQLMAHDLGG RVEGASGREY GKTQLEITAA
130 140 150 160 170 180
DPLFAGLPES IQCWMSHGDY ISAPPPGFQV TARSAYTPVA AMSDPARKLY GVQFHPEVKH
190 200 210 220 230 240
TPMGQEILRR FLFQVCGCRG DWSVSSFIED QVAAIRRQVG NGRVLCALSG GVDSSVAAAL
250 260 270 280 290 300
VHRAVGDRLT CVFVNHGLLR QGEAEQVQRA FGQAMGMNIV YVDASRRFLE KLTGVTDPEE
310 320 330 340 350 360
KRKIIGHEFI RVFEEEARKL GRVDFLVQGT LYPDVIESGT ETAAVIKSHH NVGGLPEDME
370 380 390 400 410 420
LELIEPLRLL FKDEVRRVGE ELGLPEEIVW RQPFPGPGLA IRILGEVTPE KLEILRQADA
430 440 450 460 470 480
IVTEEIRRAG LYREIWQSFA VLPSMKSVGV MGDERTYAYP IVLRAVTSDD AMTADWARLP
490 500 510
YDLLERISSR IVNEVRHINR VVYDITSKPP ATIEWE