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 O27427

Entry ID Method Resolution Chain Position Source
AF-O27427-F1 Predicted AlphaFoldDB

No variants for O27427

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O27427

No associated diseases with O27427

5 regional properties for O27427

Type Name Position InterPro Accession
domain PurM-like, C-terminal domain 186 - 339 IPR010918-1
domain PurM-like, C-terminal domain 549 - 684 IPR010918-2
domain PurM-like, N-terminal domain 60 - 174 IPR016188-1
domain PurM-like, N-terminal domain 419 - 535 IPR016188-2
domain Phosphoribosylformylglycinamidine synthase, linker domain 2 - 38 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
MVLTDSEMEF IRKELGRDPN PLEYGMLDVM FSEHCSYKSS RPVLGLFPTE GEDVIIGPGD
70 80 90 100 110 120
DAGVVEITDE LALVIGIESH NHPSAIEPYG GAGTGIGGIL RDIISMGAMP VALLDSLRFG
130 140 150 160 170 180
YLEDQKSRYL FEHVVRGISD YGNRVGVPTV AGEVEFDENF QLNPLVNVMC AGLVPKNDIK
190 200 210 220 230 240
RGIAPRPGDV FLLMGGRTGR DGIHGVTFAS EELTSSSELE DRPAVQVGDP FTKKMVMEAS
250 260 270 280 290 300
FEIMDEIEVS GVKDLGGGGL TCCISELVAK CDNGARVSLE AIPLREEGMT PYEIMLSESQ
310 320 330 340 350 360
ERMIFVMAPD DVEAAMEICR KYELPAAVIG EVTDTGRMIV ESEGEVIADL PAKLLADPPV
370 380 390 400 410 420
VEREARKPQL PEGQVEVKHP PLKDTLLKLI SSPNIASKRW VYRQYDHEVQ IRTVVKPGDD
430 440 450 460 470 480
AAVLRVDGTT GVALTVDCNS IHTKLDPYGG GAASVGEAIR NVVSMGAWPV CIVDCLNFGN
490 500 510 520 530 540
PEKPEVFWQF RECVRGMADM AETFSTPVIS GNVSFYNETE GVTVNPSPVV GVAGKLSLDS
550 560 570 580 590 600
IKTLDFKDEG EEIVVIGETG PELGASEYLR TVHGIVDGKP PETDLKAEFE AAKAVKEIID
610 620 630 640 650 660
GSGNKVTAVH DCSAGGIAVA VAEMAIKSGI GARIDPMKIP GRFRNIHEAL FSESNGRYIM
670 680 690 700 710
TVRGSARDIL GGLDVPWAVI GTTGGRTLEF GDVALDISEL DDAYHGVIEA YMST