(data stored in ACNUC7421 zone)

SWISSPROT: PURL_THEFY

ID   PURL_THEFY              Reviewed;         765 AA.
AC   Q47TL8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 92.
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=Tfu_0158;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(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; CP000088; AAZ54196.1; -; Genomic_DNA.
DR   RefSeq; WP_011290605.1; NC_007333.1.
DR   SMR; Q47TL8; -.
DR   STRING; 269800.Tfu_0158; -.
DR   PRIDE; Q47TL8; -.
DR   EnsemblBacteria; AAZ54196; AAZ54196; Tfu_0158.
DR   KEGG; tfu:Tfu_0158; -.
DR   eggNOG; ENOG4107QIK; Bacteria.
DR   eggNOG; COG0046; LUCA.
DR   HOGENOM; HOG000238227; -.
DR   KO; K01952; -.
DR   OMA; FIEPYQG; -.
DR   OrthoDB; 26038at2; -.
DR   BioCyc; TFUS269800:G1G4Q-161-MONOMER; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000000434; 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; Q47TL8.
DR   SWISS-2DPAGE; Q47TL8.
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    765       Phosphoribosylformylglycinamidine
FT                                synthase subunit PurL.
FT                                /FTId=PRO_0000236673.
FT   REGION      107    110       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   REGION      326    328       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   ACT_SITE     59     59       {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   ACT_SITE    108    108       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       106    106       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       130    130       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       282    282       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       560    560       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING      62     62       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING     104    104       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING     129    129       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     254    254       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     522    522       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING     559    559       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     562    562       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
SQ   SEQUENCE   765 AA;  80752 MW;  8B6259A626D4CA54 CRC64;
     MSEEPRFDTV AKAAATPDLP QPYTELGMKD EEYARVREIL GRRPTSAELA IYSVMWSEHC
     SYKSSKVHLR QFGEKAPDTD VLLVGIGENA GVVDVGDGYA VTFKIESHNH PSYVEPHQGA
     ATGVGGIVRD ILSMGARPVA VMDSLRFGPA DAPDTQRVLP GVVSGISSYG NCLGLPNIGG
     EVGFDAGYAS NPLVNALCVG VLKHENIKLA QASGPGNHVV LFGAATGPDG IGGASVLASA
     SFDEESQAKR PSVQVGDPFL EKLLIECCME LYAKDLVVGI QDLGAAGVSC ATTELAAGGT
     GGMRIELDRV PLRDPRLTPE EILMSESQER MMAIVEPDKL DEFLAVCAKW DILASVIGEV
     TDVTPEEEAR GGRLVMTWRG ETIVDLPPRT AADQGPVYHR PIERPADQDA LLADDPAALP
     RPSSDEELRD QVLRVLAAPG ICDSSWITDQ YDRYVMGNTV LAMPHDSGMI RIAEDTDRGV
     ALATDGNGRY TRLDPYVGTQ LAYAEAYRNV AATGARPLAV TNCLNFGSPE DPGVMWQFAE
     ATRGLADACQ ALGTPVTGGN VSFYNQTGST AINPTPVIGV LGVIDDVHKR VTSAFSAEGE
     SVVFLLGETR LELGGSAWAD VIHGHLGGRP PQIDLDAEAA LGRVLIDGAA AELLVSAHDL
     SDGGLAVALA ESCLRGGVGC EVDLGDDAFT ALFSESAARA VVSVRPEHET ALVDLCAKHG
     VPVRRLGTVG GSALTMVHRT GRISIEVAEL RDAYESTLPA LFGNK
//

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