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Database: UniProt/TrEMBL
Entry: D8GYQ1_BACAI
LinkDB: D8GYQ1_BACAI
Original site: D8GYQ1_BACAI 
ID   D8GYQ1_BACAI            Unreviewed;       739 AA.
AC   D8GYQ1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   19-FEB-2014, entry version 19.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase 2;
DE            EC=6.3.5.3;
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase II;
GN   Name=purL; OrderedLocusNames=BACI_c03380;
OS   Bacillus cereus var. anthracis (strain CI).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=637380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI;
RX   PubMed=20634886; DOI=10.1371/journal.pone.0010986;
RA   Klee S.R., Brzuszkiewicz E.B., Nattermann H., Bruggemann H., Dupke S.,
RA   Wollherr A., Franz T., Pauli G., Appel B., Liebl W., Couacy-Hymann E.,
RA   Boesch C., Meyer F.D., Leendertz F.H., Ellerbrok H., Gottschalk G.,
RA   Grunow R., Liesegang H.;
RT   "The genome of a Bacillus isolate causing anthrax in chimpanzees
RT   combines chromosomal properties of B. cereus with B. anthracis
RT   virulence plasmids.";
RL   PLoS ONE 5:E10986-E10986(2010).
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; CP001746; ADK03079.1; -; Genomic_DNA.
DR   RefSeq; YP_003790217.1; NC_014335.1.
DR   EnsemblBacteria; ADK03079; ADK03079; BACI_c03380.
DR   GeneID; 9452860; -.
DR   KEGG; bal:BACI_c03380; -.
DR   PATRIC; 42175225; VBIBacCer111781_0607.
DR   HOGENOM; HOG000238227; -.
DR   KO; K01952; -.
DR   BioCyc; BCER637380:GHO7-328-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   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   NP_BIND     111    122       ATP (By similarity).
SQ   SEQUENCE   739 AA;  80175 MW;  8BEB25939B943EFF CRC64;
     MSLMLEPNPT QIKEERIYAE MGLTDEEFAM VEKILGRLPN YTETGLFSVM WSEHCSYKNS
     KPVLRKFPTT GERVLQGPGE GAGIVDIGDN QAVVFKMESH NHPSAIEPYQ GAATGVGGII
     RDVFSMGARP VALLNSLRFG ELQSPRVKYL FEEVVAGIAG YGNCIGIPTV GGEVQFDPCY
     EGNPLVNAMC VGLINHEDIK KGQAHGAGNT VMYVGASTGR DGIHGATFAS EELSESSEAK
     RPAVQVGDPF MEKLLIEACL ELIQSDALVG IQDMGAAGLT SSSAEMASKA GMGIEMYLDD
     VPQRETGMTP YEMMLSESQE RMLIVVKKGR EQEIVDLFEK YGLAAVTMGK VTEDKMLRLF
     HKGEMVAEVP ADALAEEAPI YHKPSKEAAY FAEFQQMKME TPKVENYKET LFALLQQPTI
     ASKEWVYDQY DYQVRTSTVV TPGSDAAVVR VRGTEKGLAM TTDCNSRYIY LDPEVGGKIA
     VAEAARNIVC SGGEPLAITD CLNFGNPEKP EIFWQIEKSV DGMSEACRTL QTPVIGGNVS
     MYNERSGEAV YPTPTVGMVG LVHDLKHVTT QEFKQAGDLV YVIGETKAEF GGSELQKMLH
     GKIFGQSPSI DLDVELKRQK QVLAAIQAGL VQSAHDVAEG GLAVAISESA IGANGLGATV
     KLDGEATAAL FAESQSRFVI TVKRENKEAF EKAVEAIQVG EVTNTNEVTI HNEENEVLLT
     ANVDEMRQAW KGAIPCLLK
//
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