ID   PUR5_ALCBS              Reviewed;         347 AA.
AC   Q0VP77;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase;
DE            EC=6.3.3.1;
DE   AltName: Full=AIRS;
DE   AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
DE   AltName: Full=AIR synthase;
GN   Name=purM; OrderedLocusNames=ABO_1573;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + 2-(formamido)-N(1)-(5-phospho-D-
CC       ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)-
CC       formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the AIR synthase family.
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DR   EMBL; AM286690; CAL17021.1; -; Genomic_DNA.
DR   RefSeq; YP_693293.1; -.
DR   GeneID; 4211149; -.
DR   GenomeReviews; AM286690_GR; ABO_1573.
DR   KEGG; abo:ABO_1573; -.
DR   NMPDR; fig|393595.12.peg.1578; -.
DR   HOGENOM; Q0VP77; -.
DR   OMA; Q0VP77; CGKLDPE.
DR   BioCyc; ABOR393595:ABO_1573-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-lig...; IEA:HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00741; -; 1.
DR   InterPro; IPR000728; AIR_synth.
DR   InterPro; IPR010918; AIR_synth_C.
DR   InterPro; IPR004733; PurM_cligase.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   TIGRFAMs; TIGR00878; purM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Purine biosynthesis.
FT   CHAIN         1    347       Phosphoribosylformylglycinamidine cyclo-
FT                                ligase.
FT                                /FTId=PRO_0000258325.
SQ   SEQUENCE   347 AA;  36921 MW;  BA0167CA0E880676 CRC64;
     MTEQKRPLTY RDAGVDIDAG NELVKRIAPV AKRTRRPEVL GGLGGFGALC ELPTKYKNPV
     LVAGTDGVGT KLRLAIDHNR HEKVGVDLVA MCVNDLIVGG AEPLFFLDYY ATGKLDVEIA
     TSVVTGIGEG CELAGCALIG GETAEMPGMY EGEDYDLAGF CVGVVEKDGV LDGSKVEAGD
     KLIGLGASGP HSNGYSLIRR IMAQAETDID LDGKPLIEHL LEPTRIYVKS LLKLIEQVPV
     HAMAHITGGG LPENLPRVLP DNTRAVIDTK SWEFPAVFQW LQQEGQVPAF EMYRTFNCGV
     GMVIAVPASH VDDALALLEA EGESAFLIGE IQAGDGQPDV VLDGLSA
//