PUR9_BAUCH
ID PUR9_BAUCH Reviewed; 526 AA.
AC Q1LU51;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=BCI_0035;
OS Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX NCBI_TaxID=374463;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT sharpshooters.";
RL PLoS Biol. 4:1079-1092(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; CP000238; ABF13814.1; -; Genomic_DNA.
DR RefSeq; WP_011520246.1; NC_007984.1.
DR AlphaFoldDB; Q1LU51; -.
DR SMR; Q1LU51; -.
DR STRING; 374463.BCI_0035; -.
DR EnsemblBacteria; ABF13814; ABF13814; BCI_0035.
DR KEGG; bci:BCI_0035; -.
DR HOGENOM; CLU_016316_5_2_6; -.
DR OMA; WRVAKFV; -.
DR OrthoDB; 1049662at2; -.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR Proteomes; UP000002427; 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..526
FT /note="Bifunctional purine biosynthesis protein PurH"
FT /id="PRO_1000018847"
FT DOMAIN 1..148
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
SQ SEQUENCE 526 AA; 58384 MW; 4A77AA22AA874B48 CRC64;
MQRPIIIRRA LLSVSDKTNI CELAKSLLKR GVQLISTNGT ARLLVNAGIH VTEVSNYTGF
PEIMDGRVKT LHPKIHGGIL ARRNIDDTIM QQYKIEHIDM VVVNLYPFAE VVASATCNHE
KVVENIDIGG TALLRSAAKN YSNVVVVVSI NDYISIINEI DCNNGAVSLE TRLNLAIKAF
QHTATYDSQI KDYFTSQVYT DSSKCSSIFP PILNINFVKK QDMRYGENQH QLAAFYLDTR
NKEKSIATTK QLQGRALSYN NIADADAALE CVKEFSEPAC VIVKHINPCS VAMGKTILVA
YQRAYETDPT SAFGGVIAFN RSLDLCTAQE IIARQFIEVI IAPTVDQEAL LILAKKKNIR
VLSSGQWNKP IPNLNFRQVN GGLLVQERDL VMINLHDLRI VSQRQPTTME IQDALFCWKV
VKFVKSNAIV YARNQRTIGI GAGQMSRIDS AKIASIKAID NKLNIRGSTM ASDAFFPFRD
GLDSAAKVGV SCVIQPGGSI RDQEVITAAN EHNIAMIFTN IRHFRH
