ID   PUR9_LARHH              Reviewed;         526 AA.
AC   C1D6F1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
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};
GN   OrderedLocusNames=LHK_03208;
OS   Laribacter hongkongensis (strain HLHK9).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Laribacter.
OX   NCBI_TaxID=557598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLHK9;
RX   PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA   Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L.,
RA   Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J.,
RA   Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.;
RT   "The complete genome and proteome of Laribacter hongkongensis reveal
RT   potential mechanisms for adaptations to different temperatures and
RT   habitats.";
RL   PLoS Genet. 5:E1000416-E1000416(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-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:58467,
CC         ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; 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; CP001154; ACO76186.1; -; Genomic_DNA.
DR   RefSeq; WP_012698649.1; NC_012559.1.
DR   AlphaFoldDB; C1D6F1; -.
DR   SMR; C1D6F1; -.
DR   STRING; 557598.LHK_03208; -.
DR   GeneID; 75108387; -.
DR   KEGG; lhk:LHK_03208; -.
DR   eggNOG; COG0138; Bacteria.
DR   HOGENOM; CLU_016316_5_2_4; -.
DR   UniPathway; UPA00074; UER00133.
DR   UniPathway; UPA00074; UER00135.
DR   Proteomes; UP000002010; 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   CDD; cd01421; IMPCH; 1.
DR   Gene3D; 3.40.140.20; -; 2.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 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   NCBIfam; TIGR00355; purH; 1.
DR   PANTHER; PTHR11692:SF0; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC; 1.
DR   PANTHER; PTHR11692; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH; 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; SSF53927; Cytidine deaminase-like; 1.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 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_1000122962"
FT   DOMAIN          1..147
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
SQ   SEQUENCE   526 AA;  56135 MW;  82364408DBB769E2 CRC64;
     MTKIERALIS VSDKTGILEF ARGLAAHGVE ILSTGGTAKL LADNNVPVIE VADYTGFPEM
     LDGRVKTLHP KIHGGILGRR DLPEHVAKMA EHGIGNIDLV CVNLYPFEAT IAKEGCALED
     AIENIDIGGP TMVRSAAKNW AHVAIVTDAA DYPALLEEMG ANAGALSRAT RFDLSRKAFT
     HTAAYDGAIS NYLTAVQADQ GLAGEPVRTL FPTRLNLQVV KVQDMRYGEN PHQSAAFYRD
     LDPAPGTLAH YRQLQGKELS YNNIADSDAA WEAVKTFDDP ACVIVKHANP CGVAVAADPL
     SAYRLAFATD TTSAFGGIIA FNREVDAATV EAVSAQFLEV LIAPAFTDDA KALIAAKKNV
     RVLEVPVEAG ANRFELKRVG GGLLVQTPDI KNVTLDELKV VTKAQPTRQQ LADLLFAWRV
     AKFVKSNAIV FAAGGQTAGI GAGQMSRVDS TRIAARKAQD AGLSLKNAVA ASDAFFPFRD
     GVDVIAEQGI SAIIQPGGSM RDEEVIKAAD EHGIAMVFTG NRHFRH
//