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Protein

Phosphoribosylformylglycinamidine synthase

Gene

ADE6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (By similarity).By similarity

Catalytic activityi

ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Phosphoribosylformylglycinamidine synthase (ADE6)
  2. Bifunctional purine biosynthetic protein ADE5,7 (ADE5,7)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei719 – 7191ATP; via carbonyl oxygenBy similarity
Metal bindingi720 – 7201MagnesiumBy similarity
Metal bindingi762 – 7621MagnesiumBy similarity
Metal bindingi766 – 7661MagnesiumBy similarity
Metal bindingi930 – 9301MagnesiumBy similarity
Binding sitei932 – 9321ATPBy similarity
Active sitei1187 – 11871NucleophileBy similarity
Active sitei1319 – 13191By similarity
Active sitei1321 – 13211By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi345 – 35612ATPSequence analysisAdd
BLAST
Nucleotide bindingi424 – 4263ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • phosphoribosylformylglycinamidine synthase activity Source: SGD

GO - Biological processi

  • 'de novo' IMP biosynthetic process Source: SGD
  • glutamine metabolic process Source: GO_Central
  • purine nucleotide biosynthetic process Source: SGD
  • ribonucleoside monophosphate biosynthetic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-486.
YEAST:YGR061C-MONOMER.
ReactomeiR-SCE-73817. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00074; UER00128.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylformylglycinamidine synthase (EC:6.3.5.3)
Short name:
FGAM synthase
Short name:
FGAMS
Alternative name(s):
Formylglycinamide ribonucleotide amidotransferase
Short name:
FGAR amidotransferase
Short name:
FGAR-AT
Formylglycinamide ribotide amidotransferase
Gene namesi
Name:ADE6
Ordered Locus Names:YGR061C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR061C.
SGDiS000003293. ADE6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 13581357Phosphoribosylformylglycinamidine synthasePRO_0000100405Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP38972.

PTM databases

iPTMnetiP38972.

Interactioni

Protein-protein interaction databases

BioGridi33306. 54 interactions.
DIPiDIP-1175N.
IntActiP38972. 4 interactions.
MINTiMINT-401068.

Structurei

3D structure databases

ProteinModelPortaliP38972.
SMRiP38972. Positions 232-651.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1093 – 1358266Glutamine amidotransferase type-1Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the FGAMS family.Curated

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

GeneTreeiENSGT00390000007600.
HOGENOMiHOG000261359.
InParanoidiP38972.
KOiK01952.
OMAiHAHIEKG.
OrthoDBiEOG72890P.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00419. PurL_1.
InterProiIPR010918. AIR_synth_C_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010073. PRibForGlyAmidine_synth.
IPR016188. PurM-like_N.
[Graphical view]
PfamiPF02769. AIRS_C. 2 hits.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF56042. SSF56042. 2 hits.
TIGRFAMsiTIGR01735. FGAM_synt. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDYILPGPK ALSQFRVDNL IKDINSYTNS TSVINELRSC YIHYVNGIAQ
60 70 80 90 100
NLSEQDTKLL EVLLTYDSAL DIANDPLARQ LNDAVANNLP SSALGEDTYL
110 120 130 140 150
IRVVPRSGTI SPWSSKATNI AHVCGLQDKV QRIERGLALL IKTVPGFPLL
160 170 180 190 200
ENLNDISLKC VYDRMTQQLY LTEPPNTMSI FTHEEPKPLV HVPLTPKDTK
210 220 230 240 250
QSPKDILSKA NTELGLALDS GEMEYLIHAF VETMKRDPTD VELFMFAQVN
260 270 280 290 300
SEHCRHKIFN ADWTIDGIKQ QFTLFQMIRN THKLNPEYTI SAYSDNAAVL
310 320 330 340 350
DSENDAFFFA PNSTTKEWTS TKERIPLLIK VETHNHPTAV SPFPGAATGS
360 370 380 390 400
GGEIRDEGAT GRGSKTKCGL SGFSVSDLLI PGNEQPWELN IGKPYHIASA
410 420 430 440 450
LDIMIEAPLG SAAFNNEFGR PCINGYFRTL TTKVLNHQGK EEIRGFHKPI
460 470 480 490 500
MIAGGFGTVR PQFALKNTPI TPGSCLIVLG GQSMLIGLGG GAASSVASGE
510 520 530 540 550
GSADLDFASV QRGNPEMERR CQQVIDACVA LGNNNPIQSI HDVGAGGLSN
560 570 580 590 600
ALPELVHDND LGAKFDIRKV LSLEPGMSPM EIWCNESQER YVLGVSPQDL
610 620 630 640 650
SIFEEICKRE RAPFAVVGHA TAEQKLIVED PLLKTTPIDL EMPILFGKPP
660 670 680 690 700
KMSRETITEA LNLPEANLSE IPSLQDAIQR VLNLPSVGSK SFLITIGDRS
710 720 730 740 750
VTGLIDRDQF VGPWQVPVAD VGVTGTSLGE TIISTGEAMA MGEKPVNALI
760 770 780 790 800
SASASAKLSV AESLLNIFAA DVKSLNHIKL SANWMSPASH QGEGSKLYEA
810 820 830 840 850
VQALGLDLCP ALGVAIPVGK DSMSMKMKWD DKEVTAPLSL NITAFAPVFN
860 870 880 890 900
TSKTWTPLLN RNTDDSVLVL VDLSAKQETK SLGASALLQV YNQVGNKSPT
910 920 930 940 950
VYDNAILKGF LESLIQLHQQ KEDIVLAYHD RSDGGLLITL LEMAFASRCG
960 970 980 990 1000
LEINIDGGDL ESQLTNLFNE ELGAVFQISA KNLSKFEKIL NENGVAKEYI
1010 1020 1030 1040 1050
SIVGKPSFQS QEIKIINSTT NDVIYANSRS ELEQTWSKTS YEMQKLRDNP
1060 1070 1080 1090 1100
KTAEEEFASI TDDRDPGLQY ALTYNPADDM KIGLELSSQR PKVAILREQG
1110 1120 1130 1140 1150
VNGQMEMAWC FQQAGFNSVD VTMTDLLEGR FHLDDFIGLA ACGGFSYGDV
1160 1170 1180 1190 1200
LGAGAGWAKS VLYHEGVRSQ FSKFFNERQD TFAFGACNGC QFLSRLKDII
1210 1220 1230 1240 1250
PGCENWPSFE RNVSEQYEAR VCMVQISQEK DNSSEESVFL NGMAGSKLPI
1260 1270 1280 1290 1300
AVAHGEGKAT FSKSAEQLEK FEKDGLCCIR YVDNYGNVTE RFPFNPNGST
1310 1320 1330 1340 1350
NGIAGIKSPN GRVLAMMPHP ERVCRLEANS WYPEGKYEEW GGYGPWIRLF

RSARRWVG
Length:1,358
Mass (Da):148,905
Last modified:October 1, 1996 - v2
Checksum:iA48A24ECB1BE7973
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841A → L in AAA50357 (Ref. 1) Curated
Sequence conflicti219 – 2202DS → EC in AAA50357 (Ref. 1) Curated
Sequence conflicti226 – 2261L → V in AAA50357 (Ref. 1) Curated
Sequence conflicti492 – 4921A → P in AAA50357 (Ref. 1) Curated
Sequence conflicti499 – 4991G → R in AAA50357 (Ref. 1) Curated
Sequence conflicti551 – 5511A → T in AAA50357 (Ref. 1) Curated
Sequence conflicti604 – 6041E → K in AAA50357 (Ref. 1) Curated
Sequence conflicti1169 – 11702SQ → TSSK in AAA50357 (Ref. 1) Curated
Sequence conflicti1298 – 12981G → A in AAA50357 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14566 Genomic DNA. Translation: AAA50357.1.
Z72846 Genomic DNA. Translation: CAA97063.1.
BK006941 Genomic DNA. Translation: DAA08157.1.
PIRiS64356.
RefSeqiNP_011575.1. NM_001181190.1.

Genome annotation databases

EnsemblFungiiYGR061C; YGR061C; YGR061C.
GeneIDi852952.
KEGGisce:YGR061C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14566 Genomic DNA. Translation: AAA50357.1.
Z72846 Genomic DNA. Translation: CAA97063.1.
BK006941 Genomic DNA. Translation: DAA08157.1.
PIRiS64356.
RefSeqiNP_011575.1. NM_001181190.1.

3D structure databases

ProteinModelPortaliP38972.
SMRiP38972. Positions 232-651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33306. 54 interactions.
DIPiDIP-1175N.
IntActiP38972. 4 interactions.
MINTiMINT-401068.

PTM databases

iPTMnetiP38972.

Proteomic databases

MaxQBiP38972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR061C; YGR061C; YGR061C.
GeneIDi852952.
KEGGisce:YGR061C.

Organism-specific databases

EuPathDBiFungiDB:YGR061C.
SGDiS000003293. ADE6.

Phylogenomic databases

GeneTreeiENSGT00390000007600.
HOGENOMiHOG000261359.
InParanoidiP38972.
KOiK01952.
OMAiHAHIEKG.
OrthoDBiEOG72890P.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.
BioCyciMetaCyc:MONOMER-486.
YEAST:YGR061C-MONOMER.
ReactomeiR-SCE-73817. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

PROiP38972.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00419. PurL_1.
InterProiIPR010918. AIR_synth_C_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010073. PRibForGlyAmidine_synth.
IPR016188. PurM-like_N.
[Graphical view]
PfamiPF02769. AIRS_C. 2 hits.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF56042. SSF56042. 2 hits.
TIGRFAMsiTIGR01735. FGAM_synt. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Saccharomyces cerevisiae formylglycinamide ribonucleotide synthetase."
    Andreichuk Y.V., Domkin V.D.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPUR4_YEAST
AccessioniPrimary (citable) accession number: P38972
Secondary accession number(s): D6VUJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 40800 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.