ID   PUR9_BACTN              Reviewed;         507 AA.
AC   Q8A155;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 44.
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=BT_3812;
OS   Bacteroides thetaiotaomicron.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX   MEDLINE=22550858; PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA   Chiang H.C., Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO78917.1; -; Genomic_DNA.
DR   RefSeq; NP_812723.1; -.
DR   HSSP; P31335; 1G8M.
DR   GeneID; 1072684; -.
DR   GenomeReviews; AE015928_GR; BT_3812.
DR   KEGG; bth:BT_3812; -.
DR   NMPDR; fig|226186.1.peg.3810; -.
DR   HOGENOM; Q8A155; -.
DR   OMA; Q8A155; VILAHEY.
DR   BioCyc; BTHE226186:BT_3812-MON; -.
DR   BRENDA; 2.1.2.3; 21018.
DR   BRENDA; 3.5.4.10; 21018.
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.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Multifunctional enzyme;
KW   Purine biosynthesis; Transferase.
FT   CHAIN         1    507       Bifunctional purine biosynthesis protein
FT                                purH.
FT                                /FTId=PRO_0000192071.
SQ   SEQUENCE   507 AA;  55880 MW;  0C09966527E570E4 CRC64;
     MSESKRIKTA LVSVYHKEGL DEIITKLYEE GVEFLSTGGT RQFIESLGYP CKAVEDLTTY
     PSILGGRVKT LHPKIFGGIL CRRDLEQDIQ QIEKYEIPEI DLVIVDLYPF EATVASGASE
     ADIIEKIDIG GISLIRAAAK NYNDVIIVAS QAQYKPLLDM LMEHGATSSL EERRWMAKEA
     FAVSSHYDSA IFNYFDAGEG SAFRCSVNNQ KQLRYGENPH QKGYFYGNLD AMFDQIHGKE
     ISYNNLLDIN AAVDLIDEYE DLTFAILKHN NACGLASRPT VLEAWTDALA GDPVSAFGGV
     LITNGVIDKA AAEEINKIFF EVIIAPDYDV DALEILGQKK NRIILVRKEA KLPKKQFRAL
     LNGVLVQDKD MNIETVADLR TVTDKAPTPE EVEDLLFANK IVKNSKSNAI VLAKGKQLLA
     SGVGQTSRVD ALKQAIEKAK SFGFDLNGAV MASDAFFPFP DCVEIADKEG ITAVIQPGGS
     VKDDLTFAYC NEHGMAMVTT GIRHFKH
//