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 C5A4U6

Entry ID Method Resolution Chain Position Source
AF-C5A4U6-F1 Predicted AlphaFoldDB

No variants for C5A4U6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C5A4U6

No associated diseases with C5A4U6

5 regional properties for C5A4U6

Type Name Position InterPro Accession
domain PurM-like, C-terminal domain 184 - 339 IPR010918-1
domain PurM-like, C-terminal domain 554 - 678 IPR010918-2
domain PurM-like, N-terminal domain 59 - 172 IPR016188-1
domain PurM-like, N-terminal domain 416 - 532 IPR016188-2
domain Phosphoribosylformylglycinamidine synthase, linker domain 6 - 36 IPR041609

Functions

Description
EC Number 6.3.5.3 Carbon--nitrogen ligases with glutamine as amido-N-donor
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
magnesium ion binding Binding to a magnesium (Mg) ion.
phosphoribosylformylglycinamidine synthase activity Catalysis of the reaction: N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + ATP + H(2)O = 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate + ADP + 2 H(+) + phosphate.

1 GO annotations of biological process

Name Definition
'de novo' IMP biosynthetic process The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MFPHEEKLIR ERLGREPNEL EWAMLEVMWS EHASYKSSRP WLKLLPTENE HVILGPGEDA
70 80 90 100 110 120
GIVKFDDETW VVVGIESHNH PSAVEPYGGA ATGVGGIVRD ILCMGARPIA LLDPIRFGPL
130 140 150 160 170 180
EKERNRYLFE YVVKGIADYG NRIGVPTVGG ETEFDESLDS YTLVNVACVG IMRPEHLVHS
190 200 210 220 230 240
YVTEAGLKLI LVGNRTGRDG VHGVTFASEE LSENTEEDRS AVQIPDPFTE KLLIEATLEA
250 260 270 280 290 300
VYTGRVKALK DLGGGGLTCA ASEMAGKKGF GAVIYADRVP LREPGMTPTE VMISESQERM
310 320 330 340 350 360
LFAVKPEDVE EIGRIFEEYE LEWTVVGETI EEPRFVVYWK GEKVADLPIE LLTEVPTIEW
370 380 390 400 410 420
ELKPYSAEGP VETPDVPFER AFDLVWGSPN ILSKRWVWEQ YDHEVQGRTV LKPGRDAAVL
430 440 450 460 470 480
KINDEYGLAF VADGNPNHSY LNPYQGAMGA VAEVVRNLVS VGAEPLALVD NLNFASPERP
490 500 510 520 530 540
EVYWSFAETV RGLADAARAF GLAYVSGNVS FYNEVVDRPI KPTPVVAGLG KVKLEAIPNG
550 560 570 580 590 600
GFEEGLLIGV VGLTKPELGG SELFARLGVE GGLAPRVNLE EEKANANGVL EAIRRGLVRA
610 620 630 640 650 660
VHDVSRGGLA VALAKMAVAG NTGFTADLSK VPSETTNPIE VAFSESHGRY IVAFPEENLE
670 680 690 700 710
ELKGLFKHFV IIGRTGGSDA VFLWNGWELL RKPVSELKAV HESLPMLLGE EE