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 01-MAY-2013, entry version 42.
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; WSEHCCY; -.
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: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 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
//