ID B5Y717_COPPD Unreviewed; 738 AA.
AC B5Y717;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 01-MAY-2013, entry version 38.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase 2;
DE EC=6.3.5.3;
DE AltName: Full=Phosphoribosylformylglycinamidine synthase II;
GN Name=purL; OrderedLocusNames=COPRO5265_0194;
OS Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / BT).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermodesulfobiaceae; Coprothermobacter.
OX NCBI_TaxID=309798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35245 / DSM 5265 / BT;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Coprothermobacter proteolyticus
RT strain ATCC 5245 / DSM 5265 / BT.";
RL Submitted (AUG-2008) 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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP001145; ACI17009.1; -; Genomic_DNA.
DR RefSeq; YP_002246564.1; NC_011295.1.
DR ProteinModelPortal; B5Y717; -.
DR STRING; 309798.COPRO5265_0194; -.
DR EnsemblBacteria; ACI17009; ACI17009; COPRO5265_0194.
DR GeneID; 6944380; -.
DR KEGG; cpo:COPRO5265_0194; -.
DR PATRIC; 21473260; VBICopPro72829_0186.
DR eggNOG; COG0046; -.
DR HOGENOM; HOG000238227; -.
DR KO; K01952; -.
DR OMA; WSEHCCY; -.
DR ProtClustDB; PRK01213; -.
DR BioCyc; CPRO309798:GH7M-236-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 103 114 ATP (By similarity).
SQ SEQUENCE 738 AA; 79266 MW; 2863F526E4AC0480 CRC64;
MENSNTTPLW RTLGLTDLEY EQIVSGLGRE PNFTELAMFS VMWSEHCAYK NSKPLLKMLP
SKGQRVMQGP GENAGVLDIG DGLALVMKIE SHNHPSAVEP YQGAATGVGG IVRDIFAMGA
RPVVLMDSLR FGSLGEGRTN YLFEQVVAGI SDYGNCIGVP TVGGEIYFQD CYQKSPLVNA
LCAGIVEQDK MQTGKASGVG SPVLIVGATT GRDGIGGASF ASQELGEDAE EKLPSVQVGD
PFMEKLLIEA CLEAYETGFV VAVQDMGAAG ITSSASEMAA RGEVGMELNL DCVPLRAEGM
AAHEILISES QERMLLVVEK GKEDQIKQIM EKWGLHAAIM GRVTDDGWLR VCYHGEVVAQ
LPAQLLAEGA PQYIREGIPS EHLKDIQDLD VTALQPPADL ECTLLELLKS PNIASKAWVF
EQYDHMVRTD TVVRPGSDAA VVRIKGKHQA LAFTTDCNAT YCFLDPYEGA KAAVVEAARN
LSMVGAEPIG ITDCLNFGNP EDPAVYWQMQ RCIEGIRDAC QVLNIPVVSG NVSLYNETEL
GPIFPTPVIG CAGLIPDVSR VCTMGLKDDG DVVLVLGEDK GELGGSEYLQ VQYGLVKGKP
PVVDLEKEKA LQELVRKLIW EGLLKSAHDI SEGGLAVALA ECALCGERGV EVDLTTSLRP
DAALFSESQA RAVVSLSPQN LEAVLKLAQD YEVPAAVLGN VGGESLLIRV NGEEVADVPL
IQCAEHYWRG LEWAMKGI
//
