B2IC83

PR
Gene name
purL
Protein name
Phosphoribosylformylglycinamidine synthase subunit PurL
Names
FGAM synthase, Formylglycinamide ribonucleotide amidotransferase subunit II, FGAR amidotransferase II, FGAR-AT II, Glutamine amidotransferase PurL, Phosphoribosylformylglycinamidine synthase subunit II
Species
Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB 8712)
KEGG Pathway
bid:Bind_3119
EC number
6.3.5.3: Carbon--nitrogen ligases with glutamine as amido-N-donor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

348-417 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B2IC83

Entry ID Method Resolution Chain Position Source
AF-B2IC83-F1 Predicted AlphaFoldDB

No variants for B2IC83

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2IC83

No associated diseases with B2IC83

5 regional properties for B2IC83

Type Name Position InterPro Accession
domain PurM-like, C-terminal domain 201 - 351 IPR010918-1
domain PurM-like, C-terminal domain 567 - 700 IPR010918-2
domain PurM-like, N-terminal domain 86 - 188 IPR016188-1
domain PurM-like, N-terminal domain 437 - 553 IPR016188-2
domain Phosphoribosylformylglycinamidine synthase, linker domain 15 - 52 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
MSADPPITPE LVAAHGLKPD EYQRILTLIG REPSFTELGI FSAMWNEHCS YKSSRIHLRK
70 80 90 100 110 120
LPTKAPWVIQ GPGENAGVID IGDGEACIFK MESHNHPSYI EPHQGAATGV GGILRDVFTM
130 140 150 160 170 180
GARPVASLDL LRFGAPEHPL MRHLIAGVAS GIGSYGNSFG VPTVGGSTKF DRRYNGNILV
190 200 210 220 230 240
NAMAVGIARQ DEIFYAKATG VGNPIVYLGS KTGRDGIHGA TMASAAFEAD AQEKRPTVQV
250 260 270 280 290 300
GDPFAEKLLL EACLELMKTG AVIAIQDMGA AGLTSSAVEM GAKGNLGIEL DLDAVPCREP
310 320 330 340 350 360
GMSAYEMLLS ESQERMLMVL APEKAAEAEA VFRKWGLDFA IIGKTTDDLR FVIKHEGEIK
370 380 390 400 410 420
ADLPIKELGD EAPVYDRPSV LTPRPATIAA DTIVPPISHG EALLRLIGSP DLASKLWITE
430 440 450 460 470 480
QYDSLILGNT IQGPGGDAAL IRLGDGPKGL ALTADVTQRY CEADPYEGGK QAVTMAWRNL
490 500 510 520 530 540
TAVGALPLAV TDNLNFGNPE NPKIMGQFIG CLEGIGEACR ALDFPIVSGN VSLYNASEGQ
550 560 570 580 590 600
DIPPTPAIGG VGLLEDASRG ATLSIKRPGD AILLLGETQG WLGASLYLRD ICGREDGAPP
610 620 630 640 650 660
VVDLALEKRI GNFLRGLIAN RALTAVHTLT DGGLAVGLAK MALAGGIGAR IDIPGHCPAH
670 680 690 700 710 720
AYLFGEDQAR YLVTAAPEKA EAIRIEAEQL GIACQLIGRT GGPTLELGQE ASVAIEDLRR
730
AFEEWLPNHM TGIVIE