PUR9_CLONN
ID PUR9_CLONN Reviewed; 500 AA.
AC A0Q1J0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Bifunctional purine biosynthesis protein PurH {ECO:0000255|HAMAP-Rule:MF_00139};
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_00139};
DE EC=2.1.2.3 {ECO:0000255|HAMAP-Rule:MF_00139};
DE AltName: Full=AICAR transformylase {ECO:0000255|HAMAP-Rule:MF_00139};
DE Includes:
DE RecName: Full=IMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_00139};
DE EC=3.5.4.10 {ECO:0000255|HAMAP-Rule:MF_00139};
DE AltName: Full=ATIC {ECO:0000255|HAMAP-Rule:MF_00139};
DE AltName: Full=IMP synthase {ECO:0000255|HAMAP-Rule:MF_00139};
DE AltName: Full=Inosinicase {ECO:0000255|HAMAP-Rule:MF_00139};
GN Name=purH {ECO:0000255|HAMAP-Rule:MF_00139}; OrderedLocusNames=NT01CX_2419;
OS Clostridium novyi (strain NT).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT;
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:58467, ChEBI:CHEBI:58475; EC=2.1.2.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route):
CC step 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}.
CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC region. {ECO:0000255|HAMAP-Rule:MF_00139}.
CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000255|HAMAP-
CC Rule:MF_00139}.
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DR EMBL; CP000382; ABK61189.1; -; Genomic_DNA.
DR RefSeq; WP_011722486.1; NC_008593.1.
DR AlphaFoldDB; A0Q1J0; -.
DR SMR; A0Q1J0; -.
DR STRING; 386415.NT01CX_2419; -.
DR EnsemblBacteria; ABK61189; ABK61189; NT01CX_2419.
DR KEGG; cno:NT01CX_2419; -.
DR eggNOG; COG0138; Bacteria.
DR HOGENOM; CLU_016316_5_2_9; -.
DR OMA; WRVAKFV; -.
DR OrthoDB; 1049662at2; -.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR Proteomes; UP000008220; Chromosome.
DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.140.20; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR HAMAP; MF_00139; PurH; 1.
DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR002695; PurH-like.
DR PANTHER; PTHR11692; PTHR11692; 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 SMART; SM00851; MGS; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR TIGRFAMs; TIGR00355; purH; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Hydrolase; Multifunctional enzyme; Purine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..500
FT /note="Bifunctional purine biosynthesis protein PurH"
FT /id="PRO_1000018879"
FT DOMAIN 1..144
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
SQ SEQUENCE 500 AA; 55650 MW; FCF54E3C946C5F3C CRC64;
MLKRALISVF NKEGIVDFAK FLVNKGVEII STGGTYKHLK ENNIPVTEVN EVTGFDEILD
GRVKTLHPAI HGGILAIRDN KEHMSIIENK GIKPIDMVVV NLYPFFEKVK EDLEFQEKIE
FIDIGGPTMI RAAAKNFKDV VVLTDTKDYS DVMDQIEKNN EVNYDTRKRL AGKVFNLMAS
YDAAISNFLL EDTEYPENLA LSYTKSMDLR YGENSHQSAA CYTANNGKGI MNNIEILNGK
QLSYNNIKDM DIAWKVVWEF DDIACCGLKH NTPCGVALGE NVHDAYLKAY SCDPVSIFGG
IVAFNRKVDK KTAEEMVKIF LEIVIAPDFD SDALEVLKTK KNLRVIKCNT KPEDNFNIAK
VDGAILVQSE DKLFAEKMEV VTDKKPTEEE LKELTFAMKV CKYTKSNAIV VSKGCVAVGI
GGGQVNRIWA AEEALERGEG ATVLASDAFF PFDDVVKTAA KHGIKAIIQP GGSIRDKDSI
KACNENDISM VFTGIRHFKH
