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 B2SLG1

Entry ID Method Resolution Chain Position Source
AF-B2SLG1-F1 Predicted AlphaFoldDB

No variants for B2SLG1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2SLG1

No associated diseases with B2SLG1

5 regional properties for B2SLG1

Type Name Position InterPro Accession
domain GMP synthase, C-terminal 208 - 521 IPR001674
domain GMP synthase, glutamine amidotransferase 9 - 200 IPR004739
domain Glutamine amidotransferase 11 - 196 IPR017926
domain NAD/GMP synthase 214 - 296 IPR022310
domain GMP synthetase ATP pyrophosphatase domain 204 - 396 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
MTNIHTDKIL ILDFGAQYTQ LIARRIREIG VYCEIWAWDH DPSEIAGFGA KGIILSGGPE
70 80 90 100 110 120
STTLPGAPVA PQEVFDSGLP VFGICYGMQT LAAQLGGATE AADQREFGHA EVDVIAADAL
130 140 150 160 170 180
FAGLTDHAGA PRLNVWMSHG DHVSQVPPGF TITATTDRIP VAAMSNEDKR WYGVQFHPEV
190 200 210 220 230 240
THTLQGQTLL RRFVVDICGC QTLWTAANII DDQIARVREQ VGDDDVILGL SGGVDSSVVA
250 260 270 280 290 300
ALLHKAIGDK LTCVFVDTGL LRWQEGDQVM AMFAEHMGVK VIRVNAADRY FAKLEGVSDP
310 320 330 340 350 360
EAKRKIIGNL FVEIFDEESN TLANAKWLAQ GTIYPDVIES AGSKTGKAHV IKSHHNVGGL
370 380 390 400 410 420
PQHMKLGLVE PLRELFKDEV RRLGVELGLP RTMVYRHPFP GPGLGVRILG EVKREYAELL
430 440 450 460 470 480
AKADAIFIDE LRKADLYDKI SQAFAVFLPV KSVGVVGDAR AYEWVIALRA VETIDFMTAH
490 500 510 520
WAHLPYDFLG TVSNRIINEL RGVSRVVYDI SGKPPATIEW E