PUR4_DICDI
ID PUR4_DICDI Reviewed; 1355 AA.
AC Q54JC8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=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=purL; ORFNames=DDB_G0288145;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 164-184 AND 534-542, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
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; AAFI02000109; EAL63360.1; -; Genomic_DNA.
DR RefSeq; XP_636865.1; XM_631773.1.
DR AlphaFoldDB; Q54JC8; -.
DR SMR; Q54JC8; -.
DR STRING; 44689.DDB0230086; -.
DR PaxDb; Q54JC8; -.
DR PRIDE; Q54JC8; -.
DR EnsemblProtists; EAL63360; EAL63360; DDB_G0288145.
DR GeneID; 8626476; -.
DR KEGG; ddi:DDB_G0288145; -.
DR dictyBase; DDB_G0288145; purL.
DR eggNOG; KOG1907; Eukaryota.
DR HOGENOM; CLU_001031_0_0_1; -.
DR InParanoid; Q54JC8; -.
DR OMA; LSANWMW; -.
DR PhylomeDB; Q54JC8; -.
DR Reactome; R-DDI-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00128.
DR PRO; PR:Q54JC8; -.
DR Proteomes; UP000002195; Chromosome 5.
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; ISS:dictyBase.
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 GO; GO:0006164; P:purine nucleotide biosynthetic process; ISS:dictyBase.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing;
KW Glutamine amidotransferase; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..1355
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000327671"
FT DOMAIN 1087..1325
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 1182
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 1310
FT /evidence="ECO:0000250"
FT ACT_SITE 1312
FT /evidence="ECO:0000250"
FT BINDING 326..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 406..408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 743
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 747
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 911
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 913
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1355 AA; 149827 MW; 859E9DCBD36E5A6C CRC64;
MTIQQFYRKP AISEYEIKLL KNNLKKQHNI DIESIETEYC FNVQYPDNHK LNESEQSTLV
WLLSETFEPK NFSIDKSFLK TTTTTTENEI IIEVGPRMNF TTTYSSNATS ICKSCNLSII
DRIERSRRYL VKSVSKLSEK QIDQFLELIH DRMTECLYPT PIKSFDTGII PKAVVYIPVV
EEGRAALERV NKEMGLAFDE QDLALYTDLF QNQLKRNPSD VECFDIGQSN SEHSRHWFFN
GKLIVDGNMS DKTLFQIVKN TLKANPQNSL IAFSDNSSSI KGFKTKVLIP KSQIEASEYL
EGEREQPIIF TAETHNFPTG IAPFEGAETG TGGRLRDTHA TGRGSLVVAG TVGYCVGNLN
IPGYELPWEN KEYNYPDNMA NPLKIEIEAS NGASDYGNKF GEPVIIGFTR SYGNTLPNGE
RREWIKPIMF SGGIGFMDER HLKKEQPEIG MVVVKAGGPA YRIGMGGGSA SSMVGGDNKH
ELDFSAVQRG DAEMGQKLNR IVRSCVESEI HGGCNPIVSV HDQGAGGAGN VLKEIVDPLG
AKIYLDRIIS GDPTLSAMEI WGAEYQENDA LLIKAEHKDY LKKVSERERL PIAFVGDVTG
DGIAQLITKD GETPVNLPLD KVLQKMPPKT FVLDHVEKQL KPFTLPKELL VGDHQTCFNE
CLNRVLRLLS VGSKRFLINK VDRAVTGLVA RQQCVGPLHT PVSNVAVISS GYFGKSGAAT
SIGEQPIKGF ISAKSMAYLT VGEALTNLMW ASITDLGDVK CSGNWMWAAK LKGEGVELYD
AAIEMHDVMV ELGIAIDGGK DSLSMAAKAP KSDGSQELVK APGALVVSTY VPCDDITLTV
TPDLKLSSKD DSVILYLDLG CANNFIGGSA LTQVFNQVGN DEPHHNTPLL KNTFMAIQKL
VKQQLISAGH DRSDGGLITT LIEMSLSGNR GLEINLPDTH NSDQSPLSII KLLFSEELGA
VLEIKKSNQQ IVLDILKQFN VPTQVIGNTS CNNNNNNNNN GSDEDLFIVK VGDKLIYNIK
LSQLSKQWEE TSYQLELLQA NPTFVESEMK NLLKRATGKG KGPNYNMTYK ISPISKELAL
LANKAPKVAV IREEGSNGDR EMAAAFHFAG FQAFDVTMSD LLNGNIQLDE RFKGVAFVGG
FSYGDVMDSA KGWAGSIRFN QQVSKQFDHF YGRNDTFSLG LCNGCQLMAL LGWVPYRGIE
QTHQPRFIHN ASGRFESRWV NVKIMPSPAL LLKGMEGSVL GVWSQHGEGR FWSEDQSIVN
DIKANNLSPI RYVDDDGEIT ESYPFNPSGT QEGFASLCSK DGRHLAIMPH PERSFLSWQW
PFMPENIKQN VGGLDQPSPW IKIFQNAKSF CDSLN
