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Database: UniProt
Entry: Q19311
LinkDB: Q19311
Original site: Q19311 
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-OCT-2014, entry version 113.
DE   RecName: Full=Probable phosphoribosylformylglycinamidine synthase;
DE            Short=FGAM synthase;
DE            Short=FGAMS;
DE            EC=6.3.5.3;
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase;
DE            Short=FGAR amidotransferase;
DE            Short=FGAR-AT;
DE   AltName: Full=Formylglycinamide ribotide amidotransferase;
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   -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in
CC       the purines biosynthetic pathway. Catalyzes the ATP-dependent
CC       conversion of formylglycinamide ribonucleotide (FGAR) and
CC       glutamine to yield formylglycinamidine ribonucleotide (FGAM) and
CC       glutamate (By similarity). {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC       {ECO:0000305}.
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DR   EMBL; Z35598; CAA84656.2; -; Genomic_DNA.
DR   PIR; T20718; T20718.
DR   RefSeq; NP_497942.2; NM_065541.5.
DR   UniGene; Cel.5802; -.
DR   ProteinModelPortal; Q19311; -.
DR   SMR; Q19311; 298-587.
DR   IntAct; Q19311; 1.
DR   MINT; MINT-3386428; -.
DR   STRING; 6239.F10F2.2; -.
DR   PaxDb; Q19311; -.
DR   PRIDE; Q19311; -.
DR   EnsemblMetazoa; F10F2.2; F10F2.2; WBGene00008654.
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; PPKMSRI; -.
DR   OrthoDB; EOG7353X4; -.
DR   UniPathway; UPA00074; UER00128.
DR   NextBio; 888888; -.
DR   PRO; PR:Q19311; -.
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:UniProtKB-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   Gene3D; 3.30.1330.10; -; 2.
DR   Gene3D; 3.40.50.880; -; 2.
DR   HAMAP; MF_00419; PurL_1; 1.
DR   InterPro; IPR010918; AIR_synth_C_dom.
DR   InterPro; IPR000728; AIR_synth_N_dom.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR010073; PRibForGlyAmidine_synth.
DR   InterPro; IPR016188; PurM_N-like.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 2.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF55326; SSF55326; 2.
DR   SUPFAM; SSF56042; SSF56042; 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; Magnesium; Metal-binding; Nucleotide-binding;
KW   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. {ECO:0000255}.
FT   NP_BIND     394    396       ATP. {ECO:0000250}.
FT   ACT_SITE   1146   1146       Nucleophile. {ECO:0000250}.
FT   ACT_SITE   1280   1280       {ECO:0000250}.
FT   ACT_SITE   1282   1282       {ECO:0000250}.
FT   METAL       682    682       Magnesium. {ECO:0000250}.
FT   METAL       721    721       Magnesium. {ECO:0000250}.
FT   METAL       725    725       Magnesium. {ECO:0000250}.
FT   METAL       894    894       Magnesium. {ECO:0000250}.
FT   BINDING     681    681       ATP; via carbonyl oxygen. {ECO:0000250}.
FT   BINDING     896    896       ATP. {ECO:0000250}.
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
//
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