ID D8GYQ1_BACAI Unreviewed; 739 AA.
AC D8GYQ1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 01-MAY-2013, entry version 17.
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: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 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
//
