ID   PUR9_BUCAP              Reviewed;         526 AA.
AC   Q8KA70;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 43.
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=BUsg_032;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67603.1; -; Genomic_DNA.
DR   RefSeq; NP_660392.1; -.
DR   HSSP; P31335; 1G8M.
DR   GeneID; 1005848; -.
DR   GenomeReviews; AE013218_GR; BUsg_032.
DR   KEGG; bas:BUsg032; -.
DR   HOGENOM; Q8KA70; -.
DR   OMA; Q8KA70; VVKHVKS.
DR   BioCyc; BAPH198804:BUSG032-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    526       Bifunctional purine biosynthesis protein
FT                                purH.
FT                                /FTId=PRO_0000192077.
SQ   SEQUENCE   526 AA;  59422 MW;  7F0F13954EF902A5 CRC64;
     MSLNNIIKNA LVSLSDKTDL LKISKILAEK KINLFCTGGT ADVLKKNKIP VLEISDYTNF
     PEIMNGRLKT LHPKIIGGIL GRREKDQKIM KLHNLIPIDI VIVNFYPFEK IQNRKEFTIE
     EIIDNIDIGG PTLVRAAAKN YKDVIVIVDL SDFTSCIQLI NTNTVSLETR FDLATKAFKY
     TALYEEIISK YFLKKNPYRK KHQKNIFPNE FQLNFIKKQD LRYGENQHQK SSFYIEKEIL
     KSGTISSSNQ IQGKNLSYNN ICDADIALEC VKEFSKPTCV IVKHGNPCGV SESNSLIKAY
     FSAYNADPIS AFGGIIAFNC LLDLDTAQEI VKKQFVEVII APEIDEMAVK ILKRKKNIRL
     LICGKIEKNK KGLDFKRITN GLLIQEYDCD EINAKNFDFV TNRLPTEKEL EDAIFSWKVA
     KFVKSNAIVY SLNKTTIGIG AGQTSRIDAT KLANLKVKDR NHNNTTGATM ASDAFFPFRD
     GIDNAALIGI SCIIQPGGSI RDKEVIESAN EHNISMIFTK KRHFKH
//