Q085S1

PR
Gene name
purL
Protein name
Phosphoribosylformylglycinamidine synthase
Names
FGAM synthase, FGAMS, Formylglycinamide ribonucleotide amidotransferase, FGAR amidotransferase, FGAR-AT
Species
Shewanella frigidimarina (strain NCIMB 400)
KEGG Pathway
sfr:Sfri_1141
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)

423-496 (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 Q085S1

Entry ID Method Resolution Chain Position Source
AF-Q085S1-F1 Predicted AlphaFoldDB

No variants for Q085S1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q085S1

No associated diseases with Q085S1

4 regional properties for Q085S1

Type Name Position InterPro Accession
domain PurM-like, C-terminal domain 431 - 585 IPR010918-1
domain PurM-like, C-terminal domain 864 - 963 IPR010918-2
domain Phosphoribosylformylglycinamidine synthase, N-terminal 35 - 149 IPR040707
domain Phosphoribosylformylglycinamidine synthase, linker domain 170 - 219 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.
metal ion binding Binding to a metal 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.
glutamine metabolic process The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEIIRGAPAL SAFRVQKLME ACENAALPVS QIYAEYVHLA SLSEPLDDNE RLQLETILTY
70 80 90 100 110 120
GPAIESHAPQ GTLLFVTPRP GTISPWSSKA TDIAHNCGLG KVSRLERGIA YYVEASVLTA
130 140 150 160 170 180
EQQKLLQGLL HDRMVEVMLP AFEAAEVLFA RTEPAKFSSV NILAEGRRAL EVANIKLGLA
190 200 210 220 230 240
LADDEIDYLI ENFVRLKRNP NDIELMMFAQ ANSEHCRHKI FNADWTIDGE VQLKSLFKMI
250 260 270 280 290 300
KNTFEVTPDY VLSAYKDNAA VMTGSVAGRF FPDPDGIYNY HTEPMHILMK VETHNHPTAI
310 320 330 340 350 360
SPYPGAATGS GGEIRDEGAT GRGSKPKAGL SGFTVSNLKI PGFVQPWEGD YGKPDRIVTP
370 380 390 400 410 420
LEIMLEGPLG GAAFNNEFGR PAITGYFRTY EQLVSSHNGV EVRGYHKPIM IAGGLGNIRE
430 440 450 460 470 480
DHVQKGEITI GAKLIVLGGP AMNIGLGGGA ASSMASGQSS EDLDFASVQR ENPEMERRCQ
490 500 510 520 530 540
EVIDRCWQLG DTNPIQFIHD VGAGGLSNAF PELVNDADRG GVFNLRNVPS DEPGMSPLEI
550 560 570 580 590 600
WCNESQERYV LSVAPENLQQ FADICARERA PFAVVGEATA EMHLTLADSH FNNKPIDLPL
610 620 630 640 650 660
EVLLGKAPKM SRDVVTAKAV SPALDQTKIE LKDAVKRILT LPTVADKTFL ITIGDRSVTG
670 680 690 700 710 720
LVNRDQMVGP WQVPVADCAV TASSYDSYCG EAMSMGERTP LALLDFDASA RMAVAESIMN
730 740 750 760 770 780
IAGTDIGSFK RIKLSANWMS PAGHPGEDAG LYQAVKAIGE DLCPELGITI PVGKDSMSMK
790 800 810 820 830 840
TAWEDNGTQK TVTSPMSLVI TAFGVVQDIR KTVTPQLRSD KGDSALLMLD LSNGQNRLGG
850 860 870 880 890 900
SCLAQVYSEL GDIAPTLDKT ANLAGFFEVM QQLVADQAVM AYHDRSDGGL FTTLVEMAFA
910 920 930 940 950 960
GNTGLTIDLA SLSGTDLERL FNEEIGAVIQ VSAIDAKAIA AQFEAKGVTC HHIGGLQTAD
970 980 990 1000 1010 1020
KISINDGERV IFADSRTALR TLWSETTYRM QALRDNPECA REEYELKQQA DAPGLTVKLG
1030 1040 1050 1060 1070 1080
FNPSEDVAAP YILKGVAPKM AILREQGVNS HVEMAAAFDR AGFESRDVHM SDILSGRISL
1090 1100 1110 1120 1130 1140
EEFQGLVACG GFSYGDVLGA GEGWAKSILF NDRARDEFSR FFERDSSIAL GVCNGCQMLS
1150 1160 1170 1180 1190 1200
NLKEIIPGSE HWPRFVRNRS ERFEARFSLV EVQQNPSVFF EGMVGSRMPI AVSHGEGLVE
1210 1220 1230 1240 1250 1260
FANAQALANA EASGTIALRY VDGHGQIATQ YPENPNGSAN GLTGICTTDG RVTIMMPHPE
1270 1280 1290
RVFRTVANSW HPDNWGEDSP WMRMFRNARV KIG