ID   PUR9_BURCM              Reviewed;         521 AA.
AC   Q0BI80;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=Bamb_0584;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000440; ABI86143.1; -; Genomic_DNA.
DR   RefSeq; YP_772477.1; -.
DR   GeneID; 4308531; -.
DR   GenomeReviews; CP000440_GR; Bamb_0584.
DR   KEGG; bam:Bamb_0584; -.
DR   NMPDR; fig|339670.3.peg.3223; -.
DR   OMA; Q0BI80; 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    521       Bifunctional purine biosynthesis protein
FT                                purH.
FT                                /FTId=PRO_1000018853.
SQ   SEQUENCE   521 AA;  55521 MW;  8BA275C6EF042929 CRC64;
     MIKQALISVS DKTGIVDFAK SLSDLGVKLL STGGTAKLLA DAGLPVTEVA DYTGFPEMLD
     GRVKTLHPKV HGGILARRDL PEHMQALEQH DIPTIDLLVV NLYPFVATIA KDDCTLADAI
     ENIDIGGPTM LRSAAKNHRD VTVVVDPADY AVVLDEMKAN GNAIGYATNF RLATKVFAHT
     AQYDGAITNY LTSLTDELQH ASRSAYPATL NMAFDKVQDL RYGENPHQSA AFYRDLAAPA
     GALANYRQLQ GKELSYNNIA DSDAAWECVK TFDVPACVII KHANPCGVAV GNDSADAYAK
     AFQTDPTSAF GGIIAFNREV DEAAAQAVAK QFVEVLIAPS FSDAAKQVFA AKQNVRLLEI
     ALGDGHNAFD LKRVGGGLLV QSLDSKNVQP SELRVVTKRQ PSAKEMDDLL FAWRVAKYVK
     SNAIVFCGNG MTLGVGAGQM SRVDSARIAS IKAQNAGLTL AGSAVASDAF FPFRDGLDVV
     VAAGATCVIQ PGGSMRDDEV IAAADEHGIA MILTGVRHFR H
//