(data stored in ACNUC7421 zone)

SWISSPROT: PURL_FRASN

ID   PURL_FRASN              Reviewed;         769 AA.
AC   A8LCI3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000255|HAMAP-Rule:MF_00420};
DE            Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00420};
DE            EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00420};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000255|HAMAP-Rule:MF_00420};
DE            Short=FGAR amidotransferase II {ECO:0000255|HAMAP-Rule:MF_00420};
DE            Short=FGAR-AT II {ECO:0000255|HAMAP-Rule:MF_00420};
DE   AltName: Full=Glutamine amidotransferase PurL {ECO:0000255|HAMAP-Rule:MF_00420};
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000255|HAMAP-Rule:MF_00420};
GN   Name=purL {ECO:0000255|HAMAP-Rule:MF_00420};
GN   OrderedLocusNames=Franean1_0155;
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC       complex involved in the purines biosynthetic pathway. Catalyzes
CC       the ATP-dependent conversion of formylglycinamide ribonucleotide
CC       (FGAR) and glutamine to yield formylglycinamidine ribonucleotide
CC       (FGAM) and glutamate. The FGAM synthase complex is composed of
CC       three subunits. PurQ produces an ammonia molecule by converting
CC       glutamine to glutamate. PurL transfers the ammonia molecule to
CC       FGAR to form FGAM in an ATP-dependent manner. PurS interacts with
CC       PurQ and PurL and is thought to assist in the transfer of the
CC       ammonia molecule from PurQ to PurL. {ECO:0000255|HAMAP-
CC       Rule:MF_00420}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-D-
CC         ribosyl)glycinamide = 2-(formamido)-N(1)-(5-phospho-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:58426, ChEBI:CHEBI:58478,
CC         ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00420};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC       phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00420}.
CC   -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1
CC       PurL, 1 PurQ and 2 PurS subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00420}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}.
CC   -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00420}.
DR   EMBL; CP000820; ABW09622.1; -; Genomic_DNA.
DR   RefSeq; WP_012157599.1; NC_009921.1.
DR   SMR; A8LCI3; -.
DR   STRING; 298653.Franean1_0155; -.
DR   PRIDE; A8LCI3; -.
DR   EnsemblBacteria; ABW09622; ABW09622; Franean1_0155.
DR   KEGG; fre:Franean1_0155; -.
DR   eggNOG; ENOG4108JIU; Bacteria.
DR   eggNOG; COG0046; LUCA.
DR   HOGENOM; HOG000238227; -.
DR   KO; K01952; -.
DR   OMA; FIEPYQG; -.
DR   OrthoDB; 26038at2; -.
DR   BioCyc; FSP298653:G1G9X-153-MONOMER; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000001313; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1330.10; -; 2.
DR   Gene3D; 3.90.650.10; -; 2.
DR   HAMAP; MF_00420; PurL_2; 1.
DR   InterPro; IPR010074; PRibForGlyAmidine_synth_PurL.
DR   InterPro; IPR041609; PurL_linker.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR016188; PurM-like_N.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   PANTHER; PTHR43555; PTHR43555; 1.
DR   Pfam; PF00586; AIRS; 2.
DR   Pfam; PF02769; AIRS_C; 2.
DR   Pfam; PF18072; FGAR-AT_linker; 1.
DR   PIRSF; PIRSF001587; FGAM_synthase_II; 1.
DR   SUPFAM; SSF55326; SSF55326; 2.
DR   SUPFAM; SSF56042; SSF56042; 2.
DR   TIGRFAMs; TIGR01736; FGAM_synth_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8LCI3.
DR   SWISS-2DPAGE; A8LCI3.
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    769       Phosphoribosylformylglycinamidine
FT                                synthase subunit PurL.
FT                                /FTId=PRO_1000194825.
FT   REGION      112    115       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   REGION      337    339       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   ACT_SITE     65     65       {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   ACT_SITE    113    113       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       111    111       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       135    135       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       288    288       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       562    562       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING      68     68       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING     109    109       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING     134    134       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     260    260       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     524    524       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING     561    561       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     564    564       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
SQ   SEQUENCE   769 AA;  79937 MW;  8E536E3A03F7404E CRC64;
     MTGTPSAPTT SPDDQADGPG EGTVDRQPYR ELGLTDDEYE RIVATLGRVP TDAELAMYSV
     MWSEHCSYKS SKVHLRQFRD TPATDRLLVG MGENAGVVDV GEGLAVTFKV ESHNHPSFVE
     PYQGAATGVG GIVRDILTMG ARPIGILDPL RFGAADAPDT ARVLPGVVAG IGGYGNCLGL
     PTIGGEVVFD PVYGGNPLVN ALCVGVMPVG RVQTSAATGV GNAVVLLGAK TGRDGIGGVS
     VLASATFDEG GGPARRPSVQ VGDPFTEKIL IECCLELFDR GLVTGIQDLG GAGLTCALTE
     TTAAGIATGQ PGGMEVDLDL VPLREASMAA HEVLASESQE RMLAIVTPDA LPEVLALAER
     WGVIATNIGT VTDSGRLVVR WHGEVVVDVP PGSLADDGPV YERPLRRPAD LDLLRADAPS
     ALERPRTGDA LRATLLRMIA SPNLCSRAWV TEQYDRYVQA NTVLAQPEDA GVLRLSASGL
     GIALATDGNG RYARLDPFAG AQLALAEACR NVTAAGAEPI AVTNCLNFGS PEDPEVMWQF
     AQACAGLADA CRRLGLPVTG GNVSFYNQTG SAPIHPTPVV GVLGLFDDVT RRTPIGFTDE
     GDALLLLGDT RDEFGGSEWA WATHGHLGGT PPAVDLEREK LLGEILVGGS REGLLTAAHD
     LSEGGLAQAL VESCLRGGHG ARIELPAGAD AFVELFSESA GRAVVAVPAA EQDRFARLCA
     DRGLPCRQIG VVTDGEGGSL NVAGEFAIPL DELRAAHEGT LPRLFGRGA
//

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