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 A1SYT6

Entry ID Method Resolution Chain Position Source
AF-A1SYT6-F1 Predicted AlphaFoldDB

No variants for A1SYT6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1SYT6

No associated diseases with A1SYT6

5 regional properties for A1SYT6

Type Name Position InterPro Accession
domain GMP synthase, C-terminal 201 - 510 IPR001674
domain GMP synthase, glutamine amidotransferase 6 - 191 IPR004739
domain Glutamine amidotransferase 8 - 188 IPR017926
domain NAD/GMP synthase 202 - 277 IPR022310
domain GMP synthetase ATP pyrophosphatase domain 196 - 385 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
MDKNIHEQRI LILDFGSQYT QLIARRIREI GVYCELWSWD VDEQDIKDFA PNGIILAGGP
70 80 90 100 110 120
ESVTAEGSPR APEYVFTAGV PVLGICYGMQ TMSEQLGGSV IKGEGEGEFG YAQIEVKGAS
130 140 150 160 170 180
ELFKLIEDAV AQNGNALLDV WMSHGDKVSA IPAGFTTIAN TATCQFAAIA NEEKRFYGVQ
190 200 210 220 230 240
FHPEVTHTRQ GERMLRHFVM DICGCETLWT SSSIIEDAVA RMKAQIGDDE VILGLSGGVD
250 260 270 280 290 300
SSVVAMLLQR AIGDKLTCVF VDNGLLRLNE GQQVMDMFGD HFGLKIIHVN AEHRFLEQMA
310 320 330 340 350 360
GESDPEAKRK IIGRVFVEIF DEESKKLKNA KWLAQGTIYP DVIESAGSKT GKAQVIKSHH
370 380 390 400 410 420
NVGGLPDDME MGLVEPLREL FKDEVRKIGL ELGLPYEMLY RHPFPGPGLG VRVLGEVKKE
430 440 450 460 470 480
YCDLLRRADA IFIEELHKAD LYHKVSQAFV VFLPVRSVGV MGDCRKYDWV VSLRCVETID
490 500 510 520
FMTARWSHLP YDLIGHVSNR IINEIDGISR VVYDVSGKPP ATIEWE