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 A4SM23

Entry ID Method Resolution Chain Position Source
AF-A4SM23-F1 Predicted AlphaFoldDB

No variants for A4SM23

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4SM23

No associated diseases with A4SM23

4 regional properties for A4SM23

Type Name Position InterPro Accession
domain GMP synthase, C-terminal 208 - 520 IPR001674
domain GMP synthase, glutamine amidotransferase 10 - 198 IPR004739
domain Glutamine amidotransferase 12 - 195 IPR017926
domain GMP synthetase ATP pyrophosphatase domain 203 - 395 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
MTKDIHQHRI LILDFGSQYT QLIARRVREI GVYCELWAWD VTEEQIREFN PSGIILSGGP
70 80 90 100 110 120
ESVTEAGSPR APEYVFNAGV PVFGICYGMQ TMAEQLGGKV QSSTEREFGY AQVEVLGQTN
130 140 150 160 170 180
ALLRSIEDAI APNGNALLDV WMSHGDKVTA IPADFTTIAQ TATCPHAAMA CESKHFYGVQ
190 200 210 220 230 240
FHPEVTHTRQ GARMLEHFVK DICGCECLWT PATIIDDAVA RIREQVGDDE VILGLSGGVD
250 260 270 280 290 300
SSVVAMLVHR AIGDRLTCVF VDNGLLRLNE GEQVMEMFGD HFGLNIIKVE AEERFLSALA
310 320 330 340 350 360
GEDEPEAKRK IIGRVFVEVF DDEAKKLKNA RWLAQGTIYP DVIESAASKT GKAHVIKSHH
370 380 390 400 410 420
NVGGMPAEMK MGLVEPLREL FKDEVRRVGL ELGLPYDMLY RHPFPGPGLG VRVLGEVKKE
430 440 450 460 470 480
YCDILRRADA VFIEELRKAD LYNQVSQAFA VFLPVRSVGV MGDGRKYDWV IALRAVETID
490 500 510 520
FMTAHWAHLP YDFLGHVSNR IINEINGISR VVYDVSGKPP ATIEWE