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Database: UniProt/SWISS-PROT
Entry: PURL_THEEB
LinkDB: PURL_THEEB
Original site: PURL_THEEB 
ID   PURL_THEEB              Reviewed;         761 AA.
AC   Q8DIA7;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   29-OCT-2014, entry version 81.
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=tlr1683;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
RA   Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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: ATP + N(2)-formyl-N(1)-(5-phospho-D-
CC       ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-
CC       (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.
CC       {ECO:0000255|HAMAP-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}.
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DR   EMBL; BA000039; BAC09235.1; -; Genomic_DNA.
DR   RefSeq; NP_682473.1; NC_004113.1.
DR   RefSeq; WP_011057520.1; NC_004113.1.
DR   ProteinModelPortal; Q8DIA7; -.
DR   STRING; 197221.tlr1683; -.
DR   EnsemblBacteria; BAC09235; BAC09235; BAC09235.
DR   GeneID; 1010851; -.
DR   KEGG; tel:tlr1683; -.
DR   PATRIC; 23928742; VBITheElo119873_1764.
DR   eggNOG; COG0046; -.
DR   HOGENOM; HOG000238227; -.
DR   KO; K01952; -.
DR   OMA; QAVVFKI; -.
DR   OrthoDB; EOG6FNHHR; -.
DR   UniPathway; UPA00074; UER00128.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1330.10; -; 2.
DR   Gene3D; 3.90.650.10; -; 1.
DR   HAMAP; MF_00420; PurL_2; 1.
DR   InterPro; IPR010918; AIR_synth_C_dom.
DR   InterPro; IPR000728; AIR_synth_N_dom.
DR   InterPro; IPR010074; PRibForGlyAmidine_synth_II.
DR   InterPro; IPR016188; PurM_N-like.
DR   Pfam; PF00586; AIRS; 2.
DR   Pfam; PF02769; AIRS_C; 2.
DR   SUPFAM; SSF55326; SSF55326; 2.
DR   SUPFAM; SSF56042; SSF56042; 2.
DR   TIGRFAMs; TIGR01736; FGAM_synth_II; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    761       Phosphoribosylformylglycinamidine
FT                                synthase subunit PurL.
FT                                /FTId=PRO_0000100496.
FT   REGION       93     96       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   REGION      311    313       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   ACT_SITE     48     48       {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   ACT_SITE     94     94       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL        92     92       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       116    116       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       267    267       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       537    537       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING      51     51       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING      90     90       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING     115    115       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     239    239       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     499    499       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING     536    536       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     539    539       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
SQ   SEQUENCE   761 AA;  81412 MW;  CA1224C86FF8CE64 CRC64;
     MSQTPLVTEA EITAEGLKPQ EYTEIVRRLG RHPNRAELGM FGVMWSEHCC YKNSRLLLKQ
     FPTQGPRVLV GPGENAGVVD LGDGLRLAFK IESHNHPSAI EPFQGAATGV GGILRDIFTM
     GARPIALLNA LRFGDLKEAK TQQLVKGVVA GIAHYGNCVG VPTVGGEVYF DPCYAGNPLV
     NAMALGLMET PEIVKSAASG IGNPVLYVGS TTGRDGMGGA SFASAELTDE SMSDRPAVQV
     GDPFVEKCLI EACLEAFQTG AVVAAQDMGA AGLTCSTSEM AAKGGVGIEL DLDKVPVREQ
     GMVPYEFLLS ESQERMLFVA AQGREAELIE IFQRWGLQAV VVGRVIAEPL VRVLYRGEVA
     AEVPARALAE ETPLYERECP KEPPAYVQQA RQWSVDQLPL PARSPAEILL TLLATPSIAS
     KAWVYRQYDH EVQNNTLVFP GDGDAAVIRL RGTAKGIAAT VDCPSRYVYL DPYEGGKAAV
     AEAARNLSCV GAEPLAVTDN LNFGSPETPV GYWQLANACR GLAEACRALQ TPVTGGNVSL
     YNETIDSNGQ PQPIYPTPVV GMVGLIADLQ RVVGQGWRAT GDAIYLLGLP LTTPLSDPRL
     SLGGSEYLAQ IHGLVAGCPP QIDLDLEQRV QAVCRYGIQQ GWIASAHDLS EGGLAVALAE
     SCLSGQRGAT IQLPEGTYPR WDALLFAEGG ARILVSVPPR EQVAWEAYAQ AQLPNAWTRL
     GVVNGEDTEL CIDSCNNSPL IRVTIKELDL AWRSPLPKYL D
//
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