ID   PUR9_ANADE              Reviewed;         524 AA.
AC   Q2IKQ7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=Adeh_2468;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
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., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-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; CP000251; ABC82238.1; -; Genomic_DNA.
DR   RefSeq; YP_465675.1; -.
DR   GeneID; 3890166; -.
DR   GenomeReviews; CP000251_GR; Adeh_2468.
DR   KEGG; ade:Adeh_2468; -.
DR   HOGENOM; Q2IKQ7; -.
DR   OMA; Q2IKQ7; VVKHVKS.
DR   BioCyc; ADEH290397:ADEH_2468-MON; -.
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    524       Bifunctional purine biosynthesis protein
FT                                purH.
FT                                /FTId=PRO_1000018834.
SQ   SEQUENCE   524 AA;  55984 MW;  81A77AAAD34769E7 CRC64;
     MTRRALVSVS DKTGLVPFAR RLAALGVELL STGGTQKALA EAGVPVTGVG DYTQAPEILG
     GRVKTLHPRV HGGILYRRGL ASDEADVKAR DIPPIDLVVV NLYPFREAVA AGKPFETCVE
     EIDIGGPTMV RSAAKNSAHV GVVVDPADYD KVAAELEATR ALSDATRFYL MKKAFAHTAA
     YDAAISEYLT ARETPEAAPA HFPATLAAVY TKAYDLRYGE NPHQAGAFYR AAREPEEPSV
     AFAQVLQGKE LSYNNLLDLQ AALAGVMEFD ETACVVIKHN TPCGVSTGRT AGEAFARARE
     CDPVSAFGGI VALNRPVDEA TASELTSLFL ECVIAPGYDA AARAALAVKK NLRLLEAPRL
     GAARATWRRR PEEGRELRSI PGGLLVMDRD LGSVRREDCK VMTKRAPTEQ EWKDLLFAWK
     VVKHVKSNAI VFAKDDRTVA IGGGQTSRVE SVKTAVMKAA LDVRGSSVGS DAFFPFADGV
     EEIIKAGATA IIQPGGSMRD AEVIAAADKA GIAMVATGMR HFRH
//