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Database: UniProt/SWISS-PROT
Entry: PURL_ANAVT
LinkDB: PURL_ANAVT
Original site: PURL_ANAVT 
ID   PURL_ANAVT              Reviewed;         777 AA.
AC   Q3M6Z4;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   29-OCT-2014, entry version 63.
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=Ava_3636;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000117; ABA23242.1; -; Genomic_DNA.
DR   RefSeq; YP_324137.1; NC_007413.1.
DR   ProteinModelPortal; Q3M6Z4; -.
DR   STRING; 240292.Ava_3636; -.
DR   EnsemblBacteria; ABA23242; ABA23242; Ava_3636.
DR   GeneID; 3679270; -.
DR   KEGG; ava:Ava_3636; -.
DR   PATRIC; 35428441; VBIAnaVar43351_4753.
DR   eggNOG; COG0046; -.
DR   HOGENOM; HOG000238227; -.
DR   KO; K01952; -.
DR   OMA; DHMVGTD; -.
DR   OrthoDB; EOG6FNHHR; -.
DR   BioCyc; AVAR240292:GCY3-3682-MONOMER; -.
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   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.
FT   CHAIN         1    777       Phosphoribosylformylglycinamidine
FT                                synthase subunit PurL.
FT                                /FTId=PRO_0000236646.
FT   REGION       95     98       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   REGION      313    315       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   ACT_SITE     50     50       {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   ACT_SITE     96     96       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL        94     94       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       118    118       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       269    269       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   METAL       558    558       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING      53     53       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING      92     92       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING     117    117       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     241    241       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     520    520       ATP. {ECO:0000255|HAMAP-Rule:MF_00420}.
FT   BINDING     557    557       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
FT   BINDING     560    560       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00420}.
SQ   SEQUENCE   777 AA;  83320 MW;  D21EB57A49164600 CRC64;
     MTATSPAPFS PQEIAAEGIK PEEYAEIVRR LGRHPNKAEL GMFGVMWSEH CCYKNSRPLL
     KQFPTTGPRI LVGPGENAGV VDLGEGLQLA FKIESHNHPS AVEPFQGAAT GVGGILRDIF
     TMGARPIALL NSLRFGSLED PKTQRLFSGV VAGISHYGNC VGVPTVGGEV YFDPAYSGNP
     LVNVMALGLM ETPEIVKSGA SGIGNPVLYV GSTTGRDGMG GASFASAELS DESIDDRPAV
     QVGDPFLEKS LIEACLEAFK TGAVVAAQDM GAAGITCSTS EMAAKGGVGI ELDLDKIPVR
     ETGMIPYEYL LSESQERMLF VAHKGREQEL IDIFHRWGLQ AVVAGTVIAE PIVRILFQGA
     IAAEIPADAL AENTPLYERE LLAEPPEYAR QAWEWSSDSL PTCTTAGIEI QGNLQSWQEI
     LLTLLNTPTI ASKNWVYRQY DHQVQNNTVF LPGGADAAVV RLRPLEGQGK ITNTLSGVAA
     TVDCNPRYVY LDPYEGAKAV VAEAARNLSC VGAEPLAVTD NLNFGSPEKP IGYWQLSEAC
     RGLAEGCREL ATPVTGGNVS LYNETLDPQG NPQPIYPTPV VGMVGLITDL TKICGQGWQT
     PGDVIYLLGA SITTLGASEY LATIHDTVAG RPPRVDFDLE RRVQKVCREG IYADWVRSAH
     DCAEGGLVVA LAESCLAGNL GAEIHLDASG SQLQRLDEVL FGEGGARILV SVASTQQENW
     ESYLQEHLGQ NWQKLGIVGN TDADLAVLTT DNQSLIRVSI EEMNDRYQNA IARRLAL
//
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