Q71YP9

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
Listeria monocytogenes serotype 4b (strain F2365)
KEGG Pathway
lmf:LMOf2365_1794
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)

1-44 (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 Q71YP9

Entry ID Method Resolution Chain Position Source
AF-Q71YP9-F1 Predicted AlphaFoldDB

No variants for Q71YP9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q71YP9

No associated diseases with Q71YP9

5 regional properties for Q71YP9

Type Name Position InterPro Accession
domain PurM-like, C-terminal domain 207 - 361 IPR010918-1
domain PurM-like, C-terminal domain 577 - 713 IPR010918-2
domain PurM-like, N-terminal domain 91 - 193 IPR016188-1
domain PurM-like, N-terminal domain 446 - 563 IPR016188-2
domain Phosphoribosylformylglycinamidine synthase, linker domain 11 - 57 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.

2 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.
purine ribonucleotide biosynthetic process The chemical reactions and pathways resulting in the formation of a purine ribonucleotide, a compound consisting of ribonucleoside (a purine base linked to a ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPNMEPTTKE IKEQKIYQEM GLTDSEYELV CSILGREPNY TETGLFSVMW SEHCSYKNSK
70 80 90 100 110 120
PVLRKFPTEG KQVLQGPGEG AGIVDIGDGL GVAFKVESHN HPSYVEPYQG AATGVGGIIR
130 140 150 160 170 180
DVFSMGARPI AMLNSLRFGE LDTPHAKYLV SEVVAGIAGY GNSIGIPTVG GEIQFDPCYT
190 200 210 220 230 240
KNPLVNAMCV GLIEAKDIQK GQAKGIGNPV MYVGAKTGRD GIHGATFASV EFSEEGEQQR
250 260 270 280 290 300
SAVQVGDPFM EKLLLEACLD VIRDHSDILV GIQDMGAAGL VSSSSEMASK AGAGLELIMD
310 320 330 340 350 360
DVPQRELNMT PYEMLLSESQ ERMLLCVKKG HVEEIQALFE RYGLEAVVIG QVTDDKMYKI
370 380 390 400 410 420
IHHGEVVANV PVDALAEDAP VYHKPSKEPA RYQAFQEEES FVPVMEDVVG VWKELLAQPT
430 440 450 460 470 480
IASKRHIYEQ YDYQVRTDTA VVPGSDAAIV RVRGTEKAIA MTTDCNSRYL YLDPKVGGAI
490 500 510 520 530 540
AVAEAARNIV CSGGKPLAIT DGLNFGNPEK PEIFWEIEKA ADGISAACLE LDTPVISGNV
550 560 570 580 590 600
SLYNETDGTG IYPTPVIGMV GLVEDLAHIT TQDFKNSGDV IFLIGETKAE YSGSELQKLQ
610 620 630 640 650 660
QGKISGRAPE LDLTTEKKYQ QLLLTAIQEG LVASSHDLAE GGFGVALAEA TFKAGLGADV
670 680 690 700 710 720
EVPFELNQLF SESQSRFLVS VKPENEAAFA QLMELEKVYR LGVVTEDDTI RVKHKEDQVT
730
AKTTELRSIW QGAIPCLLK