ID G2TJ47_BACCO Unreviewed; 749 AA.
AC G2TJ47;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 03-APR-2013, entry version 11.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase 2;
DE EC=6.3.5.3;
DE AltName: Full=Phosphoribosylformylglycinamidine synthase II;
GN Name=purL; ORFNames=Bcoa_1613;
OS Bacillus coagulans 36D1.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=345219;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=36D1;
RA Rhee M.S., Moritz B.E., Xie G., Copeland A., Lucas S., Lapidus A.,
RA Barry K., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Chertkov O., Brettin T., Han C., Detter C., Pitluck S., Richardson P.,
RA Land M.L., Patel M., Ou M., Harbrucker R., Ingram L.O.,
RA Shanmugam K.T.;
RT "Complete Genome Sequence of a thermotolerant sporogenic lactic acid
RT bacterium, Bacillus coagulans strain 36D1.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=36D1;
RA Shanmugan K.T.;
RL Submitted (SEP-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; CP003056; AEP00810.1; -; Genomic_DNA.
DR RefSeq; YP_004859590.1; NC_016023.1.
DR ProteinModelPortal; G2TJ47; -.
DR EnsemblBacteria; AEP00810; AEP00810; Bcoa_1613.
DR GeneID; 11171899; -.
DR KEGG; bag:Bcoa_1613; -.
DR KO; K01952; -.
DR BioCyc; BCOA345219:GH5A-1591-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; Cytoplasm; Ligase; Nucleotide-binding;
KW Purine biosynthesis.
FT NP_BIND 111 122 ATP (By similarity).
SQ SEQUENCE 749 AA; 81069 MW; 77AA7B49342597E2 CRC64;
MPLLLEPGPA EIKSQKIYRE IGLTDEEFAR VEAILGRTPN YTETGLFAVM WSEHCSYKNS
KPVLKKFPVK GERVLQGPGE GAGIIDIGDG LAVVFKIESH NHPSAIEPYQ GAATGVGGII
RDVFSMGARP VALLNSLRFG ELDSPRVKHL FKEVVAGIAG YGNCIGIPTV GGEVAFDPCY
DGNPLVNAMC VGLIEHKDIQ KGQARGIGNT VMYVGAKTGR DGIHGATFAS GQLSEDSDEK
RPAVQVGDPF MEKLLLEACL ELVRHDALVG IQDMGAAGLI SSSSEMASKA GVGLVMNLDR
IPQRETGMTP YEMMLSESQE RMLIVVKKGR EPEIIRLFQK YGLDAVAIGT VTDDKRLKLY
HHGELVADVP ADALAEDAPV YHKPSKEPAY FAAYQVMKPQ IPAVENLQET FFQLLKQPTI
ASKEWVYEQY DYQVRTNTVV MPGSDAAVIR IRGTRKALAM TTDCNARYVY LDPETGGKIA
VAEAARNIVC SGAQPLGVTD CLNFGAPEKP EIFWQLEKAA DGMSEACRAL ETPVIGGNVS
LYNETLQKTG NGEVSVQAVY PTPIVGMVGL LEDITHATTQ TFKQAGDLIY LIGEAKPEFG
GSELQKLTDG QISGKPPALD LETEARREHQ LLAAIQSGLV QSAHDVSEGG FAPALAECLF
GTENLGAHVV LKGNPVTALF SETQSRFIVS VKKEHQQVFQ NLVNEAVWIG HVTDDKQMTI
KGENGETWIL ADTAECETAW KGALRCLLK
//
