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 B7JXM2

Entry ID Method Resolution Chain Position Source
AF-B7JXM2-F1 Predicted AlphaFoldDB

No variants for B7JXM2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B7JXM2

No associated diseases with B7JXM2

4 regional properties for B7JXM2

Type Name Position InterPro Accession
domain GMP synthase, C-terminal 224 - 542 IPR001674
domain GMP synthase, glutamine amidotransferase 30 - 216 IPR004739
domain Glutamine amidotransferase 31 - 211 IPR017926
domain GMP synthetase ATP pyrophosphatase domain 219 - 417 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
MTTQTPPITN PSEKLPTEPI NKALNRQMLV ILDFGSQYSE LIARRIRETQ VYSEVLSYRT
70 80 90 100 110 120
TIEQIRQLNP RGIILSGGPN SVYDNRAPQC DPEIFHLGVP ILGVCYGMQL MVQQLGGQVE
130 140 150 160 170 180
RAKRGEYGKA SLFIDDPTDL LTNVEDGSTM WMSHGDSCTQ LPEGFDILAH TENTSCAAIA
190 200 210 220 230 240
HHQKKLFGVQ FHPEVVHSVG GIALIRNFVY HICQCEPTWT TEAFVEESIR EIRAKVGDKR
250 260 270 280 290 300
VLLALSGGVD SSTLAFLLHR AIGDNLTCMF IDQGFMRKGE PERLVEIFDK QFHIPVEYVN
310 320 330 340 350 360
ARTRFLEQLA GVTDPETKRR LIGHEFIQVF EEESERLGPF DYLAQGTLYP DVIESADTNV
370 380 390 400 410 420
DPQTGERVAV KIKSHHNVGG LPKNLRFKLV EPLRKLFKDE VRKLGRAIGL PEEIVRRHPF
430 440 450 460 470 480
PGPGLAIRII GEVTAERLNI LRDADFIVRD EISKQGMYHD FWQAFAVLLP VRSVGVMGDR
490 500 510 520 530 540
RTYAHPIVLR LITSEDGMTA DWAKVPYDLL ETISNRIVNE VKGVNRVVYD ITSKPPGTIE
WE