A5VHT8

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
Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri)
KEGG Pathway
lre:Lreu_0140
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)

352-421 (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 A5VHT8

Entry ID Method Resolution Chain Position Source
AF-A5VHT8-F1 Predicted AlphaFoldDB

No variants for A5VHT8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A5VHT8

No associated diseases with A5VHT8

5 regional properties for A5VHT8

Type Name Position InterPro Accession
domain PurM-like, C-terminal domain 207 - 359 IPR010918-1
domain PurM-like, C-terminal domain 577 - 707 IPR010918-2
domain PurM-like, N-terminal domain 90 - 193 IPR016188-1
domain PurM-like, N-terminal domain 446 - 563 IPR016188-2
domain Phosphoribosylformylglycinamidine synthase, linker domain 10 - 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.

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
MKQAMTPEEI KEKKPYLDWS LTEAEYDYIR TQLLGRLPNY TETGLFSAMW SEHCSYKKSK
70 80 90 100 110 120
PVLRLFPNKN ERVLQGPGEG AGVVDIDDGQ AVVFKAESHN HPTTVEPYQG AATGVGGILR
130 140 150 160 170 180
DIFSMGARPI ASLDSLHFGE LDNSTTRMKV TNTVRGIGDY GNCMGIPTIA GETTFDPCYQ
190 200 210 220 230 240
GNILCNAMSV GLMDQKDIQQ GRAAGIGNAV MYVGAKTGRD GIHGATFASA DFNDENMTQR
250 260 270 280 290 300
SAVQVGNPFM EKLLLEACLD LIRNHPDWLV GIQDMGAAGI VSSSAEMASE GQSGMELNLD
310 320 330 340 350 360
LVPQREPGMS AYEIMLSESQ ERMLLCVKKG HEEDVKKIFD FYDLEAVTIG RITAGHDYVL
370 380 390 400 410 420
FHDGEEVCHI PVSSLTDDVL EEESLEKKPA RIELAEQQPA WIPDIDNVAE VLTALLAQST
430 440 450 460 470 480
IADKSSLYQQ YDSQVRTNTV AGPGSDAGVL RIRGTHKGLA MTTDGNGRFV YLSPEVGGQI
490 500 510 520 530 540
ALVEAAANII ASGAEPLAIT DCLNYGDPTD PEIFWELHQS VQGMADACRE FNTPVISGNV
550 560 570 580 590 600
SLYNENNGQA IHPTPMVGMV GLIKNIDRVI PSFVQHPGDK VYLVGQTRDD YAGSELQKMM
610 620 630 640 650 660
TGDISGIVES FDLHHVHQYM QRLLTTMENG LVSSAHDLSE GGLGVALAET VFKTDLGLKI
670 680 690 700 710 720
DLADQHTARL FSETPGRFIV TVAPEKATEF EQVLGKDAHL IGEVTNSHWL MVKLANGELN
730 740
ENVAKLQETW EEAIPCQLKS KD