ID PUR4_CAEEL Reviewed; 1324 AA.
AC Q19311;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 01-MAY-2013, entry version 102.
DE RecName: Full=Probable phosphoribosylformylglycinamidine synthase;
DE Short=FGAM synthase;
DE Short=FGAMS;
DE EC=6.3.5.3;
DE AltName: Full=Formylglycinamide ribotide amidotransferase;
DE Short=FGARAT;
DE AltName: Full=Formylglycinamide ribotide synthetase;
GN ORFNames=F10F2.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for
RT investigating biology.";
RL Science 282:2012-2018(1998).
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 -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS
CC family.
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR EMBL; Z35598; CAA84656.2; -; Genomic_DNA.
DR PIR; T20718; T20718.
DR RefSeq; NP_497942.2; NM_065541.5.
DR ProteinModelPortal; Q19311; -.
DR SMR; Q19311; 298-587.
DR MINT; MINT-3386428; -.
DR STRING; 6239.F10F2.2; -.
DR PaxDb; Q19311; -.
DR EnsemblMetazoa; F10F2.2; F10F2.2; F10F2.2.
DR GeneID; 175608; -.
DR KEGG; cel:CELE_F10F2.2; -.
DR UCSC; F10F2.2; c. elegans.
DR CTD; 175608; -.
DR WormBase; F10F2.2; CE44312; WBGene00008654; -.
DR eggNOG; COG0046; -.
DR GeneTree; ENSGT00390000007600; -.
DR HOGENOM; HOG000261358; -.
DR InParanoid; Q19311; -.
DR OMA; TVKAVGM; -.
DR UniPathway; UPA00074; UER00128.
DR NextBio; 888888; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR010918; AIR_synth_C_dom.
DR InterPro; IPR000728; AIR_synth_N_dom.
DR InterPro; IPR017926; GATASE_1.
DR InterPro; IPR010073; PRibForGlyAmidine_synth.
DR InterPro; IPR016188; PurM_N-like.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 2.
DR SUPFAM; SSF56042; AIR_synth_C; 2.
DR SUPFAM; SSF55326; PurM_N-like; 2.
DR TIGRFAMs; TIGR01735; FGAM_synt; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Glutamine amidotransferase;
KW Ligase; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1 1324 Probable
FT phosphoribosylformylglycinamidine
FT synthase.
FT /FTId=PRO_0000100402.
FT DOMAIN 1053 1295 Glutamine amidotransferase type-1.
FT NP_BIND 314 325 ATP (Potential).
FT ACT_SITE 1146 1146 For GATase activity (By similarity).
SQ SEQUENCE 1324 AA; 146259 MW; C6ECB88C5FAA3797 CRC64;
MTKFHVKLYA KAVESRKLDQ IQKDFEKKFN RKIDVSVEYC YHVITQEPEL ISSNWEKLVT
LLSHSPFETS VWKESQLHPE HGKNIEIGPR TAVKTAACTN ILSIFESSGI KNVERIERGI
RYLVEDDVDV NEFFEIAADK MTEAIYGNDV KFDDESHQIE KVFLIDVLES KQNLIKANEE
LGLALDQLDL DFYYDFFVNK VKKNPTDVEL FDLAQSDSEH SRHWFFRGEI WIDDRKRDGS
LMKTIRETLD SSNDNSLIAF CDNSSAIRGF ESVCRLRPND PTTVSPMIAI FPPSHLIYSA
ETHNFPTAVC PFQGATTGTG GRIRDIHATG RGAYEIAGTV GYSFGNLNLP GLPLPWEDET
FEYPTSISEP AKIAIEASNG ASDYGNKFGE PVISGFARSF GQRLENGERC EYLKPIMFSG
GIGAIDKDEV RKEPCAPHQK VVKIGGPVYR IGVGGGAASS VSVQGNRENQ LDFAAVQRGD
AEMGGKLHRV VRACAERIGG NPLMAIHDQG AGGNGNVIKE LVEGCGVTVK SDTFQLGDES
ISLRELWTAE YQENDAALVD ASLLDALQTI SKREKCHVSV VGEVEKEQRV KLLGKSGEIA
VDLDTRQLGE REKKVFKLKS APRVLKKLEL PENLTVRKAL KRVLMLPSVA SKRYLTCKVD
RSVTGLVAQQ QCVGPLHTPL ADVAVVALSH FDTVGGAVSL GEQPIKMLID AEKGARMCIA
ETIMNLIWAP ITDLKDVKMS GNWMWAAKCD GEGARLVDAV GALCRGLREI GCAIDGGKDS
LSMAVTAHGE VVKSPGTLVL SAYAPCTNVT KVVNPSLKAV PGSKILWIKI GSSEEKMRLG
GSALAQVYSQ IGDDCPDIEN FSEISKVFSI VQQLLNREEL AGPLRKPIIL AGHDISDGGL
LTAILEMAFA GNVSIDIDIK PPNQNIKPID ILFAEECGIL LEVSNPENVL HIFSEAGIKC
QEIGKASAVF GPDAHVKIHV NGHLEINEKL VDLREEWELV GDRLGEFQTN PKSLKEAREV
RRTCQKINYK CDFDWYYNPA FIHNEQYFST APRVAIIREE GSNGDREMAS AFTLAGFQTF
DVTMTDILAG HTLEAYRGVA FVGGFSYADV LGSAKGWAAG VQFNESVSKQ FEAFRSRPDT
FSYGVCNGCQ LMAQLGWIGD EEQKGPTVFL DENECGRFDS SFGPVKIEKN VSIMLSGMEN
SVLGLWSSHG EGRFTYRNLQ NFQNLKTNGQ VCIRFCDDRG MTGADHGSVK LPYPWNPNGS
IDDVAAICSR DGRHLAMMPH ADRSFLTWQW AESSEVPWNA RFDQKTVALS PWIKMFRNAY
NWCL
//
