ID   PUR9_BAUCH              Reviewed;         526 AA.
AC   Q1LU51;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Bifunctional purine biosynthesis protein purH;
DE   Includes:
DE     RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase;
DE              EC=2.1.2.3;
DE     AltName: Full=AICAR transformylase;
DE   Includes:
DE     RecName: Full=IMP cyclohydrolase;
DE              EC=3.5.4.10;
DE     AltName: Full=Inosinicase;
DE     AltName: Full=IMP synthetase;
DE     AltName: Full=ATIC;
GN   Name=purH; OrderedLocusNames=BCI_0035;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
CC   -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + 5-amino-1-(5-
CC       phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-
CC       formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
CC   -!- CATALYTIC ACTIVITY: IMP + H(2)O = 5-formamido-1-(5-phospho-D-
CC       ribosyl)imidazole-4-carboxamide.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl
CC       THF route): step 1/1.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC       carboxamide: step 1/1.
CC   -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC       region (By similarity).
CC   -!- SIMILARITY: Belongs to the purH family.
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DR   EMBL; CP000238; ABF13814.1; -; Genomic_DNA.
DR   RefSeq; YP_588513.1; -.
DR   GeneID; 4056143; -.
DR   GenomeReviews; CP000238_GR; BCI_0035.
DR   KEGG; bci:BCI_0035; -.
DR   HOGENOM; Q1LU51; -.
DR   OMA; Q1LU51; VVKHVKS.
DR   GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:HAMAP.
DR   GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide for...; IEA:HAMAP.
DR   GO; GO:0006188; P:IMP biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00139; -; 1.
DR   InterPro; IPR002695; AICARFT_IMPCHas.
DR   InterPro; IPR013982; AICARFT_IMPCHas_formly.
DR   InterPro; IPR011607; MGS.
DR   PANTHER; PTHR11692; AICARFT_IMPCHas; 1.
DR   Pfam; PF01808; AICARFT_IMPCHas; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
DR   SMART; SM00798; AICARFT_IMPCHas; 1.
DR   TIGRFAMs; TIGR00355; purH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Multifunctional enzyme;
KW   Purine biosynthesis; Transferase.
FT   CHAIN         1    526       Bifunctional purine biosynthesis protein
FT                                purH.
FT                                /FTId=PRO_1000018847.
SQ   SEQUENCE   526 AA;  58384 MW;  4A77AA22AA874B48 CRC64;
     MQRPIIIRRA LLSVSDKTNI CELAKSLLKR GVQLISTNGT ARLLVNAGIH VTEVSNYTGF
     PEIMDGRVKT LHPKIHGGIL ARRNIDDTIM QQYKIEHIDM VVVNLYPFAE VVASATCNHE
     KVVENIDIGG TALLRSAAKN YSNVVVVVSI NDYISIINEI DCNNGAVSLE TRLNLAIKAF
     QHTATYDSQI KDYFTSQVYT DSSKCSSIFP PILNINFVKK QDMRYGENQH QLAAFYLDTR
     NKEKSIATTK QLQGRALSYN NIADADAALE CVKEFSEPAC VIVKHINPCS VAMGKTILVA
     YQRAYETDPT SAFGGVIAFN RSLDLCTAQE IIARQFIEVI IAPTVDQEAL LILAKKKNIR
     VLSSGQWNKP IPNLNFRQVN GGLLVQERDL VMINLHDLRI VSQRQPTTME IQDALFCWKV
     VKFVKSNAIV YARNQRTIGI GAGQMSRIDS AKIASIKAID NKLNIRGSTM ASDAFFPFRD
     GLDSAAKVGV SCVIQPGGSI RDQEVITAAN EHNIAMIFTN IRHFRH
//