PUR9_ECOLI
ID PUR9_ECOLI Reviewed; 529 AA.
AC P15639; Q2M8U3;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 168.
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=ATIC;
DE AltName: Full=IMP synthase;
DE AltName: Full=Inosinicase;
GN Name=purH; OrderedLocusNames=b4006, JW3970;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2687276; DOI=10.1016/s0021-9258(19)30072-9;
RA Aiba A., Mizobuchi K.;
RT "Nucleotide sequence analysis of genes purH and purD involved in the de
RT novo purine nucleotide biosynthesis of Escherichia coli.";
RL J. Biol. Chem. 264:21239-21246(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2192230; DOI=10.1111/j.1365-2958.1990.tb00605.x;
RA Flannigan K.A., Hennigan S.H., Vogelbacker H.H., Gots J.S., Smith J.M.;
RT "Purine biosynthesis in Escherichia coli K12: structure and DNA sequence
RT studies of the purHD locus.";
RL Mol. Microbiol. 4:381-392(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
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 -!- 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 -!- 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.
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.
CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC region. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000305}.
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DR EMBL; J05126; AAA24454.1; -; Genomic_DNA.
DR EMBL; X51950; CAA36212.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43104.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76980.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77313.1; -; Genomic_DNA.
DR PIR; B34193; DTECPH.
DR RefSeq; NP_418434.1; NC_000913.3.
DR RefSeq; WP_001187559.1; NZ_SSZK01000047.1.
DR AlphaFoldDB; P15639; -.
DR SMR; P15639; -.
DR BioGRID; 4262461; 76.
DR BioGRID; 852797; 1.
DR IntAct; P15639; 7.
DR STRING; 511145.b4006; -.
DR iPTMnet; P15639; -.
DR SWISS-2DPAGE; P15639; -.
DR jPOST; P15639; -.
DR PaxDb; P15639; -.
DR PRIDE; P15639; -.
DR EnsemblBacteria; AAC76980; AAC76980; b4006.
DR EnsemblBacteria; BAE77313; BAE77313; BAE77313.
DR GeneID; 948503; -.
DR KEGG; ecj:JW3970; -.
DR KEGG; eco:b4006; -.
DR PATRIC; fig|1411691.4.peg.2704; -.
DR EchoBASE; EB0788; -.
DR eggNOG; COG0138; Bacteria.
DR HOGENOM; CLU_016316_5_2_6; -.
DR InParanoid; P15639; -.
DR OMA; WRVAKFV; -.
DR PhylomeDB; P15639; -.
DR BioCyc; EcoCyc:AICARTRANSIMPCYCLO-CPLX; -.
DR BioCyc; MetaCyc:AICARTRANSIMPCYCLO-CPLX; -.
DR BRENDA; 2.1.2.3; 2026.
DR BRENDA; 3.5.4.10; 2026.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR PRO; PR:P15639; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003937; F:IMP cyclohydrolase activity; IBA:GO_Central.
DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Hydrolase; Multifunctional enzyme;
KW Purine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..529
FT /note="Bifunctional purine biosynthesis protein PurH"
FT /id="PRO_0000192091"
FT DOMAIN 1..148
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT MOD_RES 287
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
SQ SEQUENCE 529 AA; 57329 MW; DC034ED01915DA68 CRC64;
MQQRRPVRRA LLSVSDKAGI VEFAQALSAR GVELLSTGGT ARLLAEKGLP VTEVSDYTGF
PEMMDGRVKT LHPKVHGGIL GRRGQDDAIM EEHQIQPIDM VVVNLYPFAQ TVAREGCSLE
DAVENIDIGG PTMVRSAAKN HKDVAIVVKS SDYDAIIKEM DDNEGSLTLA TRFDLAIKAF
EHTAAYDSMI ANYFGSMVPA YHGESKEAAG RFPRTLNLNF IKKLDMRYGE NSHQQAAFYI
EENVKEASVA TATQVQGKAL SYNNIADTDA ALECVKEFAE PACVIVKHAN PCGVAIGNSI
LDAYDRAYKT DPTSAFGGII AFNRELDAET AQAIISRQFV EVIIAPSASE EALKITAAKQ
NVRVLTCGQW GERVPGLDFK RVNGGLLVQD RDLGMVGAEE LRVVTKRQPS EQELRDALFC
WKVAKFVKSN AIVYAKNNMT IGIGAGQMSR VYSAKIAGIK AADEGLEVKG SSMASDAFFP
FRDGIDAAAA AGVTCVIQPG GSIRDDEVIA AADEHGIAML FTDMRHFRH
