ID A8EVB3_ARCB4 Unreviewed; 737 AA.
AC A8EVB3;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 01-MAY-2013, entry version 47.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase 2;
DE EC=6.3.5.3;
DE AltName: Full=Phosphoribosylformylglycinamidine synthase II;
GN Name=purL; OrderedLocusNames=Abu_1639;
OS Arcobacter butzleri (strain RM4018).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Arcobacter.
OX NCBI_TaxID=367737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM4018;
RX PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G.,
RA Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.;
RT "The complete genome sequence and analysis of the
RT Epsilonproteobacterium Arcobacter butzleri.";
RL PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV67886.1; -; Genomic_DNA.
DR RefSeq; YP_001490556.1; NC_009850.1.
DR ProteinModelPortal; A8EVB3; -.
DR STRING; 367737.Abu_1639; -.
DR EnsemblBacteria; ABV67886; ABV67886; Abu_1639.
DR GeneID; 5623498; -.
DR KEGG; abu:Abu_1639; -.
DR PATRIC; 20964640; VBIArcBut20197_1611.
DR eggNOG; COG0046; -.
DR HOGENOM; HOG000238227; -.
DR KO; K01952; -.
DR OMA; WSEHCCY; -.
DR ProtClustDB; PRK01213; -.
DR BioCyc; ABUT367737:GHWO-1675-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 105 116 ATP (By similarity).
SQ SEQUENCE 737 AA; 79761 MW; 36D88E431F0585B9 CRC64;
MQKKEMNIQE IALAHSLTLE EFENIKEILG REPNYVEIGI FSAMWSEHCS YKSSKKYLSG
FPTKAPWVIQ GPGENAGVID IGDGYAAVFK MESHNHPSFI EPYQGAATGV GGILRDVFTM
GARPIANMNS IRFASIEGDS ETAQKHRYLL KGVVAGIGGY GNCMGVPTIG GETTFEECYA
GNNLVNAFTL GLAKADEIFY GKAEGIGNPV MYVGSKTGRD GLGGAVMSSA AFDEDSESKR
PTVQVGDPFT EKLLLEACLE LFKADLIVGI QDMGAAGLTS SSFEMAGRSG SGMIMHLDKV
PAREEGMTPY DFMLSESQER MLICAKKGCE QAIIDIFQKW ELDVAVIGEV TATGNMELFW
HGEKVAEVPV QPVSEQAPIL DRPVKKPAYL DGIENISLDK ELSNQVVFDE LFSDMEVVDK
SWVYSQYDSM VQTNTIKGPG SLDGSSIRIK ETGKALSMSA DCNTRFCYIN PELGAAAAVM
ESGRNVAMTG AVPKAITDCL NFGNPTNPEV MWQFKECCEG IKKACKDLNT PVIGGNVSLY
NETNGVGVFP TPSIAMVGVN DDANKVLPSK LQENGNILYL LGETKSEFGG SLYLKKLYGK
VAGVHPEVSF EKELALWNTV IEANKLGLLK AAKDVNVGGI AIALAKMAVV GNKGIEVNIS
LNDSKDIFSE SLSRAIVEVN PSNCEAFEKI AKSFGLECTK IGVVKGNKIS INDIYKDLDK
VSDVYFNRFK QVIEQVS
//
