ID   PUR5_CHRSD              Reviewed;         358 AA.
AC   Q1QVP5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=Csal_2112;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000285; ABE59463.1; -; Genomic_DNA.
DR   RefSeq; YP_574162.1; -.
DR   GeneID; 4029257; -.
DR   GenomeReviews; CP000285_GR; Csal_2112.
DR   KEGG; csa:Csal_2112; -.
DR   NMPDR; fig|290398.4.peg.2128; -.
DR   HOGENOM; Q1QVP5; -.
DR   OMA; Q1QVP5; MAENAYS.
DR   BioCyc; CSAL290398:CSAL_2112-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    358       Phosphoribosylformylglycinamidine cyclo-
FT                                ligase.
FT                                /FTId=PRO_0000258346.
SQ   SEQUENCE   358 AA;  37887 MW;  BFEAEF3A2DC47866 CRC64;
     MTRSSDTPSS SRASLSYKDA GVDIDAGNAL VERIKGVAKR TSRPEVMGGL GGFGALCQLP
     TGYREPVLVS GTDGVGTKLR LAMDLARHDT IGIDLVAMCV NDLVVAGAEP LFFLDYYATG
     KLDVDIAADV VTGIGEGCAQ AGCALIGGET AEMPGMYAGS DYDLAGFCVG VVEKSEILDG
     SRVAEGDVLL GLASSGPHSN GYSLIRKIIE RGQADLEQEI DGIPLRDALL APTRIYVKSL
     LSLIKESDVT VHALSHITGG GLLENVPRVL PDTLAARIDA ASWTRPAVFD WLQREGNVDE
     HEMHRVLNCG IGMVVVVPAA QAERAQAALE AAGETVHRLG EIVPRQDEEE QVRLENVR
//