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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   14-MAY-2014, entry version 60.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase 2;
DE            EC=6.3.5.3;
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase II;
DE            Short=FGAM synthase II;
GN   Name=purL; 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   -!- 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   -!- 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.
CC   -!- SUBUNIT: Heterodimer of two subunits, PurQ and PurL (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the FGAMS family.
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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-SubCell.
DR   GO; GO:0005524; F:ATP 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; Nucleotide-binding;
KW   Purine biosynthesis.
FT   CHAIN         1    777       Phosphoribosylformylglycinamidine
FT                                synthase 2.
FT                                /FTId=PRO_0000236646.
FT   NP_BIND     107    118       ATP (Potential).
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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