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Database: UniProt/TrEMBL
Entry: G7W096_PAETH
LinkDB: G7W096_PAETH
Original site: G7W096_PAETH 
ID   G7W096_PAETH            Unreviewed;       747 AA.
AC   G7W096;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   03-APR-2013, entry version 10.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase 2;
DE            EC=6.3.5.3;
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase II;
GN   Name=purL; OrderedLocusNames=HPL003_11785;
OS   Paenibacillus terrae (strain HPL-003).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=985665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPL-003;
RA   Shin S.H., Kim S., Kim J.Y.;
RT   "Complete sequence of Paenibacillus terrae HPL-003.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HPL-003;
RA   Shin S.H., Kim S., Kim J.Y.;
RL   Submitted (NOV-2011) 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; CP003107; AET59114.1; -; Genomic_DNA.
DR   RefSeq; YP_005075337.1; NC_016641.1.
DR   EnsemblBacteria; AET59114; AET59114; HPL003_11785.
DR   GeneID; 11583657; -.
DR   KEGG; pta:HPL003_11785; -.
DR   KO; K01952; -.
DR   OMA; WSEHCCY; -.
DR   UniPathway; UPA00074; UER00128.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
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; SSF56042; AIR_synth_C; 2.
DR   SUPFAM; SSF55326; PurM_N-like; 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   NP_BIND     114    125       ATP (By similarity).
SQ   SEQUENCE   747 AA;  79954 MW;  3AADADBA41202182 CRC64;
     MAQQVSAKEP TAEQVAEHKL YQQMGVSDSE YALICEFMGR QPNYTEIGVF SVMWSEHCAY
     KNSKPLLRRF PTSGPRVLMG PGEGAGIVDI GDNQAVVFKI ESHNHPSAVE PFQGAATGVG
     GIIRDIFSMG ARPVAVLNSL RFGKLESDRV KYLFEHVVSG IAGYGNCIGI PTVGGEVVFD
     ESYEGNPLVN AMCVGLIDHD KIQRGVAKGV GNPVFYVGPP TGRDGIHGAT FASVELTEES
     EANRTAVQVG DPFMEKLVME SCLELIDSGI VLGIQDMGAA GLTCSSAEMA SKAGNGLELY
     LDQVPQREEG MTPYEMMLSE SQERMLFVVE PKDEAQALEI FERWGVICAK VGKVTDDGRL
     RLFHHGDVVG DMPVTALVDE CPIYDKPSEV PAYYEQNAAI DTLRYAEVTD LNGALKKVLS
     SPSVASKKWV YEQYDYMVRT STAVRPGSDA AVVTVRGTRK GLAMTTDCNG RYVYLDPEVG
     GRIAVSEAAR NIVCSGGEPL AITDNLNFGN PEKPDIFWQM EKAVDGMAEA CRVLDTPVIG
     GNVSLYNENA KGSIYPTPVV GMVGLVHDTD HITTQGFKAE GDVIFLVGET KAELGGSEFQ
     AVVHGVSEGR PPELDLNVEK KLLNAVLSAI QTGLVQSAHD LAEGGLAVAL AESGISGGLG
     AQVNVETTLR PDHALFSESQ SRILLSASPD KASALEAHLR GLGVPVTVLG KVEGSQLTVE
     VNGQPALNEA VASLKQIWED VIPCLMK
//
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