ID   PUR9_ANASK              Reviewed;         524 AA.
AC   B4UJ61;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=AnaeK_1391;
OS   Anaeromyxobacter sp. (strain K).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC   unclassified Anaeromyxobacter.
OX   NCBI_TaxID=447217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G.,
RA   Beliaev A.;
RT   "Complete sequence of Anaeromyxobacter sp. K.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001131; ACG72622.1; -; Genomic_DNA.
DR   RefSeq; WP_012525443.1; NC_011145.1.
DR   AlphaFoldDB; B4UJ61; -.
DR   SMR; B4UJ61; -.
DR   EnsemblBacteria; ACG72622; ACG72622; AnaeK_1391.
DR   KEGG; ank:AnaeK_1391; -.
DR   HOGENOM; CLU_016316_5_2_7; -.
DR   OMA; WRVAKFV; -.
DR   OrthoDB; 1049662at2; -.
DR   UniPathway; UPA00074; UER00133.
DR   UniPathway; UPA00074; UER00135.
DR   Proteomes; UP000001871; 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; Transferase.
FT   CHAIN           1..524
FT                   /note="Bifunctional purine biosynthesis protein PurH"
FT                   /id="PRO_1000096039"
FT   DOMAIN          1..144
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
SQ   SEQUENCE   524 AA;  55969 MW;  9E4BB6528D87F982 CRC64;
     MTRRALVSVS DKTGLVPFAR RLAALGVELL STGGTQKTLA EAGVPVVGVG DYTQAPEILG
     GRVKTLHPRV HGGILYRRGL ASDEADVKAR DIPPIDLVVV NLYPFREAVA AGKPFETCVE
     EIDIGGPTMV RSAAKNSAHV GVVVDPADYE KVAAELEATR TLSAATRFYL MKKAFAHTAA
     YDAAISEYLT AREAPEAAPA HFPATLAAVY TKAYDLRYGE NPHQAGAFYR AAREPEEPSV
     AFADVLQGKE LSYNNLLDLQ AALAGVMEFD ETACVIIKHN TPCGVSTGRT AGEAFARARE
     CDPVSAFGGI VALNRPVDEA TASELTSLFL ECVIAPGYDA AARAALAVKK NLRLLEAPRL
     GAARATWRRR PEEGRELRSI PGGLLVMDRD LGSVRRDDCK VMTKRAPTEQ EWKDLLFAWK
     VVKHVKSNAI VFAKDDRTVA IGGGQTSRVE SVKTAVMKAA LDVRGSSVGS DAFFPFADGV
     EEIIKAGATA IIQPGGSMRD AEVIAAADKA GIAMVATGMR HFRH