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 A3MKQ7

Entry ID Method Resolution Chain Position Source
AF-A3MKQ7-F1 Predicted AlphaFoldDB

No variants for A3MKQ7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A3MKQ7

No associated diseases with A3MKQ7

2 regional properties for A3MKQ7

Type Name Position InterPro Accession
domain Septum formation inhibitor MinC, C-terminal 131 - 231 IPR005526
domain Septum formation inhibitor MinC, N-terminal 9 - 79 IPR007874

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
MHDKILILDF GSQVTQLIAR RVREAHVYCE IHPNDVSDDF VREFAPKGVI LSGSHASTYE
70 80 90 100 110 120
DHQLRAPQAV WDLGVPVLGI CYGMQTMAVQ LGGKVEWSDH REFGYAEVRA HGRTRLLDGI
130 140 150 160 170 180
QDFATPEGHG MLKVWMSHGD KVGEMPPGFA LMASTPSCPI AGMADEARGY YAVQFHPEVT
190 200 210 220 230 240
HTVQGRKLLE RFVLDIAGAK PDWIMRDHIE EAVARIREQV GDEEVILGLS GGVDSSVAAA
250 260 270 280 290 300
LIHRAIGDQL TCVFVDHGLL RLNEGKMVLD MFEGRLHAKV VHVDASEQFL GHLAGVADPE
310 320 330 340 350 360
HKRKIIGREF VEVFQAEAKK LTNAKWLAQG TIYPDVIESG GAKTKKATTI KSHHNVGGLP
370 380 390 400 410 420
ETLGLKLLEP LRDLFKDEVR ELGVALGLPA EMVYRHPFPG PGLGVRILGE VKRDYAELLR
430 440 450 460 470 480
RADAIFIEEL RGTLATEQDA AAGLCEPSQV GKSWYDLTSQ AFAVFLPVKS VGVMGDGRTY
490 500 510 520 530
DYVAALRAVQ TTDFMTAHWA HLPYALLGRA SNRIINEVRG INRVVYDVSG KPPATIEWE