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 C1D0M2

Entry ID Method Resolution Chain Position Source
AF-C1D0M2-F1 Predicted AlphaFoldDB

No variants for C1D0M2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C1D0M2

No associated diseases with C1D0M2

5 regional properties for C1D0M2

Type Name Position InterPro Accession
domain GMP synthase, C-terminal 196 - 511 IPR001674
domain GMP synthase, glutamine amidotransferase 3 - 187 IPR004739
domain Glutamine amidotransferase 5 - 182 IPR017926
domain NAD/GMP synthase 207 - 275 IPR022310
domain GMP synthetase ATP pyrophosphatase domain 191 - 386 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
MSVVILDFGS QFTRLIARRF RELGAYSVIL PGTASLERIG QENPQGIVLS GGPSSVYDER
70 80 90 100 110 120
APRPAPGVLE LDVPILGVCY GMQFLAHEAG GDVKRAGKRE YGKADLTRYG GQLFEGIQGE
130 140 150 160 170 180
FVAWMSHSDS VTQLPAGYEV VAETEDTPVT AIENPVSRRY GVQFHPEVVH TPKGGQLLAN
190 200 210 220 230 240
FLKICDVKRD WTAAHIVEEL IADVQHQVGD SGRVLLGISG GVDSSTLALL LARAVGERLT
250 260 270 280 290 300
AVFIDHGLLR LGEREQVEAA LRPLGVNLVT VDAREEFLGS LRGVSDPEQK RKIIGREFIR
310 320 330 340 350 360
AFERETAKLG DFDFLAQGTL YPDVIESAGG HHGDKSGAAN IKSHHNVGGL PEDLKFKLVE
370 380 390 400 410 420
PFRTLFKDEV REIAQLLGLP DHIRMRHPFP GPGLAIRCLG EVTEEKLEIL KRVDDIFISG
430 440 450 460 470 480
LREFGLYDGC SQALAVLTPI QSVGVMGDER TYSYTVALRA VTTDDYMTAE WARLPYEFLA
490 500 510
TMSNRIVNQV HEVNRVVYDI TGKPPATIEW E