ID   PUR9_CAUCR              Reviewed;         529 AA.
AC   Q9ABY4;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JUN-2009, entry version 46.
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=CC_0086;
OS   Caulobacter crescentus (Caulobacter vibrioides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=155892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   MEDLINE=21173698; PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J.,
RA   Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J.,
RA   Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L.,
RA   Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK22073.1; -; Genomic_DNA.
DR   PIR; E87259; E87259.
DR   RefSeq; NP_418905.1; -.
DR   HSSP; P31335; 1G8M.
DR   GeneID; 944147; -.
DR   GenomeReviews; AE005673_GR; CC_0086.
DR   KEGG; ccr:CC_0086; -.
DR   NMPDR; fig|190650.1.peg.85; -.
DR   TIGR; CC_0086; -.
DR   HOGENOM; Q9ABY4; -.
DR   OMA; Q9ABY4; VVKHVKS.
DR   BRENDA; 2.1.2.3; 2191.
DR   BRENDA; 3.5.4.10; 2191.
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    529       Bifunctional purine biosynthesis protein
FT                                purH.
FT                                /FTId=PRO_0000192081.
SQ   SEQUENCE   529 AA;  55238 MW;  86196441DCD993D9 CRC64;
     MPAAPDYPSA PDLVAPKRAL LSVSDKTGLV DAAKILHAAG VELVSTGGTK AAIAAAGVPV
     KDVSDLTGFP EMMDGRVKTL HPVVHGGLLG VRDAADHAKA MADHGIGGID ILYVNLYPFE
     ATVAKGGSYA ECVENIDIGG PAMIRSAAKN HGYVAVCTDP SDLAEVLEAL KAGGTTLALR
     QQLAARAYAR TAAYDAAISA WFAEALGQDF PARKSIAGTL RQTMRYGENP HQKAAFYTFP
     NPRPGVATAT QLQGKELSYN NINDTDAAFE LIAEFDPAAG PAVAIIKHAN PCGVAVGATQ
     REAYERALAC DPTSAFGGIV AVNSRLTREA AEAMVEIFTE VVIAPEADED AIAVFAAKKN
     LRLLVTGGLP DALSTGDTFK SVAGGFLVQS RDDARIKASD LKIVTQRQPT EEEVRDMLFA
     FTVGKHVKSN AIVYARAGQT LGVGAGQMNR KDSARIAALR AADFGLDLKG CACASEAFFP
     FADGLIQAAE AGATAIIQPG GSMRDPEVIE AADKLGLTMA FTGVRVFRH
//