PUR4_CAEEL
ID PUR4_CAEEL Reviewed; 1324 AA.
AC Q19311;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Probable phosphoribosylformylglycinamidine synthase;
DE Short=FGAM synthase;
DE Short=FGAMS;
DE EC=6.3.5.3;
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase;
DE Short=FGAR amidotransferase;
DE Short=FGAR-AT;
DE AltName: Full=Formylglycinamide ribotide amidotransferase;
GN Name=pfas-1 {ECO:0000312|WormBase:F10F2.2};
GN ORFNames=F10F2.2 {ECO:0000312|WormBase:F10F2.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the
CC purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of
CC formylglycinamide ribonucleotide (FGAR) and glutamine to yield
CC formylglycinamidine ribonucleotide (FGAM) and glutamate (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC ChEBI:CHEBI:456216; EC=6.3.5.3;
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000305}.
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DR EMBL; BX284603; CAA84656.2; -; Genomic_DNA.
DR PIR; T20718; T20718.
DR RefSeq; NP_497942.2; NM_065541.5.
DR AlphaFoldDB; Q19311; -.
DR SMR; Q19311; -.
DR BioGRID; 40844; 7.
DR IntAct; Q19311; 1.
DR MINT; Q19311; -.
DR STRING; 6239.F10F2.2; -.
DR iPTMnet; Q19311; -.
DR EPD; Q19311; -.
DR PaxDb; Q19311; -.
DR PeptideAtlas; Q19311; -.
DR PRIDE; Q19311; -.
DR EnsemblMetazoa; F10F2.2.1; F10F2.2.1; WBGene00008654.
DR GeneID; 175608; -.
DR KEGG; cel:CELE_F10F2.2; -.
DR UCSC; F10F2.2; c. elegans.
DR CTD; 175608; -.
DR WormBase; F10F2.2; CE44312; WBGene00008654; pfas-1.
DR eggNOG; KOG1907; Eukaryota.
DR GeneTree; ENSGT00390000007600; -.
DR HOGENOM; CLU_001031_0_0_1; -.
DR InParanoid; Q19311; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 38224at2759; -.
DR PhylomeDB; Q19311; -.
DR Reactome; R-CEL-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00128.
DR PRO; PR:Q19311; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00008654; Expressed in material anatomical entity and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1330.10; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.650.10; -; 2.
DR HAMAP; MF_00419; PurL_1; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR010073; PurL_large.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR036604; PurS-like_sf.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR SUPFAM; SSF82697; SSF82697; 1.
DR TIGRFAMs; TIGR01735; FGAM_synt; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glutamine amidotransferase; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..1324
FT /note="Probable phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100402"
FT DOMAIN 1053..1295
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 1146
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 1280
FT /evidence="ECO:0000250"
FT ACT_SITE 1282
FT /evidence="ECO:0000250"
FT BINDING 314..325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 394..396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 681
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 682
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 721
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 725
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 894
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 896
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1324 AA; 146259 MW; C6ECB88C5FAA3797 CRC64;
MTKFHVKLYA KAVESRKLDQ IQKDFEKKFN RKIDVSVEYC YHVITQEPEL ISSNWEKLVT
LLSHSPFETS VWKESQLHPE HGKNIEIGPR TAVKTAACTN ILSIFESSGI KNVERIERGI
RYLVEDDVDV NEFFEIAADK MTEAIYGNDV KFDDESHQIE KVFLIDVLES KQNLIKANEE
LGLALDQLDL DFYYDFFVNK VKKNPTDVEL FDLAQSDSEH SRHWFFRGEI WIDDRKRDGS
LMKTIRETLD SSNDNSLIAF CDNSSAIRGF ESVCRLRPND PTTVSPMIAI FPPSHLIYSA
ETHNFPTAVC PFQGATTGTG GRIRDIHATG RGAYEIAGTV GYSFGNLNLP GLPLPWEDET
FEYPTSISEP AKIAIEASNG ASDYGNKFGE PVISGFARSF GQRLENGERC EYLKPIMFSG
GIGAIDKDEV RKEPCAPHQK VVKIGGPVYR IGVGGGAASS VSVQGNRENQ LDFAAVQRGD
AEMGGKLHRV VRACAERIGG NPLMAIHDQG AGGNGNVIKE LVEGCGVTVK SDTFQLGDES
ISLRELWTAE YQENDAALVD ASLLDALQTI SKREKCHVSV VGEVEKEQRV KLLGKSGEIA
VDLDTRQLGE REKKVFKLKS APRVLKKLEL PENLTVRKAL KRVLMLPSVA SKRYLTCKVD
RSVTGLVAQQ QCVGPLHTPL ADVAVVALSH FDTVGGAVSL GEQPIKMLID AEKGARMCIA
ETIMNLIWAP ITDLKDVKMS GNWMWAAKCD GEGARLVDAV GALCRGLREI GCAIDGGKDS
LSMAVTAHGE VVKSPGTLVL SAYAPCTNVT KVVNPSLKAV PGSKILWIKI GSSEEKMRLG
GSALAQVYSQ IGDDCPDIEN FSEISKVFSI VQQLLNREEL AGPLRKPIIL AGHDISDGGL
LTAILEMAFA GNVSIDIDIK PPNQNIKPID ILFAEECGIL LEVSNPENVL HIFSEAGIKC
QEIGKASAVF GPDAHVKIHV NGHLEINEKL VDLREEWELV GDRLGEFQTN PKSLKEAREV
RRTCQKINYK CDFDWYYNPA FIHNEQYFST APRVAIIREE GSNGDREMAS AFTLAGFQTF
DVTMTDILAG HTLEAYRGVA FVGGFSYADV LGSAKGWAAG VQFNESVSKQ FEAFRSRPDT
FSYGVCNGCQ LMAQLGWIGD EEQKGPTVFL DENECGRFDS SFGPVKIEKN VSIMLSGMEN
SVLGLWSSHG EGRFTYRNLQ NFQNLKTNGQ VCIRFCDDRG MTGADHGSVK LPYPWNPNGS
IDDVAAICSR DGRHLAMMPH ADRSFLTWQW AESSEVPWNA RFDQKTVALS PWIKMFRNAY
NWCL
