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 B9L0W3

Entry ID Method Resolution Chain Position Source
AF-B9L0W3-F1 Predicted AlphaFoldDB

No variants for B9L0W3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B9L0W3

No associated diseases with B9L0W3

5 regional properties for B9L0W3

Type Name Position InterPro Accession
domain GMP synthase, C-terminal 212 - 525 IPR001674
domain GMP synthase, glutamine amidotransferase 10 - 205 IPR004739
domain Glutamine amidotransferase 12 - 199 IPR017926
domain NAD/GMP synthase 217 - 256 IPR022310
domain GMP synthetase ATP pyrophosphatase domain 208 - 400 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
MSRLLPSTTN QHPTSPSFDS VVILDYGSQY AQLIARRVRD AHVYCELVPY DTDWSALKHL
70 80 90 100 110 120
SPKGIILSGG PASVYEPDAP QLPSWVLESG LPVLGICYGM QLLAHTLGGR VAPAQRREYG
130 140 150 160 170 180
PAVVERVADH PIFAGLPARF DVWMSHGDRI DALPPGFEVL ARSANAPYAA MARDHLIGLQ
190 200 210 220 230 240
FHPEVAHTPL GSVILRNFLF DVCGCAPTWT AESFVEQAIR EIRERVGKDR VLLALSGGVD
250 260 270 280 290 300
SSVAAALIHR AIGDQLTPVF VDTGLLREGE AETIREVFGR HFRMPLVAID ARQRFLVRLR
310 320 330 340 350 360
GVSDPEQKRR LIGEEFVRVF EEIARSQGPF RFLAQGTLYP DVIESAAPGA SRTAAKIKTH
370 380 390 400 410 420
HNVGGLPQDL EFELLEPLRY LFKDEVRAIG RLLGLPEEIV QRQPFPGPGL AVRILGEVTE
430 440 450 460 470 480
EALAIVRRAD TIVREEVEAA GLSDGLWQFF AVLLPVHSTG VMGDQRTYAR VIAIRAVTST
490 500 510 520
DAMTADWARL PHDLLARLAN RIVNEVPGVN RVVYDITSKP PATIEWE