ID   PUR5_COLP3              Reviewed;         346 AA.
AC   Q47Z78;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, 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=CPS_3196;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ25488.1; -; Genomic_DNA.
DR   RefSeq; YP_269892.1; -.
DR   GeneID; 3519204; -.
DR   GenomeReviews; CP000083_GR; CPS_3196.
DR   KEGG; cps:CPS_3196; -.
DR   NMPDR; fig|167879.3.peg.2832; -.
DR   TIGR; CPS_3196; -.
DR   HOGENOM; Q47Z78; -.
DR   OMA; Q47Z78; CGKLDPE.
DR   BioCyc; CPSY167879:CPS_3196-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    346       Phosphoribosylformylglycinamidine cyclo-
FT                                ligase.
FT                                /FTId=PRO_0000258348.
SQ   SEQUENCE   346 AA;  36849 MW;  D2E9B0EFE11AC0DC CRC64;
     MSEQKQSLSY KDAGVDIDAG NALVENIKGA VKRTTRPEVM GGLGGFGSVC QLPTGYKEPV
     LVAGTDGVGT KLRLAIDLAK HDTVGIDLVA MCVNDLIVQG AEPLFFLDYY ATAKLDVAVA
     SSVVEGIAEG CIQSGCALVG GETAEMPGMY HKGDYDIAGF CVGVAEKSRL IDGTNVAAGD
     QLIALGASGP HSNGFSLIRK VLEVNNTDTN ELLEGKKIAD HLLEPTKIYV KSVLELLKNV
     DVHALSHITG GGFWENIPRV LPETAQAVIK GDSWQWPSIF NWLQENGNIT EHEMYRTFNC
     GVGMVIVVPA DKVAQSIEVL TAHGENAWHL GEIADKADGE EQVVFA
//