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Database: UniProt/SWISS-PROT
Entry: PURL_BACWK
LinkDB: PURL_BACWK
Original site: PURL_BACWK 
ID   PURL_BACWK              Reviewed;         739 AA.
AC   A9VRF1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   19-FEB-2014, entry version 45.
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=BcerKBAB4_0275;
OS   Bacillus weihenstephanensis (strain KBAB4).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B.,
RA   Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H.,
RA   Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P.,
RA   Weissenbach J., Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY41541.1; -; Genomic_DNA.
DR   RefSeq; YP_001643169.1; NC_010184.1.
DR   ProteinModelPortal; A9VRF1; -.
DR   STRING; 315730.BcerKBAB4_0275; -.
DR   EnsemblBacteria; ABY41541; ABY41541; BcerKBAB4_0275.
DR   GeneID; 5840445; -.
DR   KEGG; bwe:BcerKBAB4_0275; -.
DR   PATRIC; 19004950; VBIBacWei55973_0839.
DR   eggNOG; COG0046; -.
DR   HOGENOM; HOG000238227; -.
DR   KO; K01952; -.
DR   OMA; SQERMLF; -.
DR   OrthoDB; EOG6FNHHR; -.
DR   ProtClustDB; PRK01213; -.
DR   BioCyc; BWEI315730:GHRU-348-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   CHAIN         1    739       Phosphoribosylformylglycinamidine
FT                                synthase 2.
FT                                /FTId=PRO_1000194822.
FT   NP_BIND     111    122       ATP (Potential).
SQ   SEQUENCE   739 AA;  80338 MW;  51E4D6552E30EA1B 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
     HKDEMVAEVP ADALAEEAPI YHKPSKEAAY FAEFQQMKME TPKVEDYKET LLALLQQPTI
     ASKEWVYDQY DYQVRTSTIV TPGSDAAVIR VRGTEKGLAM TTDCNSRYIY LDPEVGGKIA
     VAEAARNIVC SGGEPLAITD CLNFGNPEKP EIFWQIEKSV DGMSEACRKL QTPVIGGNVS
     MYNERSGEAV YPTPTVGMVG LVHDLKHVTT QEFKQAGDLV YVIGETKAEF GGSELQKMIY
     GKIFGQSPSI DLDVELKRQK QVLAAIQAGL VQSAHDVAEG GLAVAITESA IGAKGLGATV
     KLDGEATAVL FAESQSRFVI TVKRENKEAF EKAVEAIQVG EVTNTNEVTI HNEENEVLLT
     ANVDEMRKAW KGAIPCLLK
//
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