ID   PUR9_STRSU              Reviewed;         515 AA.
AC   Q9F1T4;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 86.
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};
OS   Streptococcus suis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DAT1 / Serotype 2;
RX   PubMed=11133943; DOI=10.1128/jb.183.2.500-511.2001;
RA   Sekizaki T., Otani Y., Osaki M., Takamatsu D., Shimoji Y.;
RT   "Evidence for horizontal transfer of the SsuDAT1I restriction-modification
RT   genes to the Streptococcus suis genome.";
RL   J. Bacteriol. 183:500-511(2001).
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; AB045609; BAB20827.1; -; Genomic_DNA.
DR   RefSeq; WP_002935323.1; NZ_VKJM01000010.1.
DR   AlphaFoldDB; Q9F1T4; -.
DR   SMR; Q9F1T4; -.
DR   STRING; 996306.SSUR61_1393; -.
DR   eggNOG; COG0138; Bacteria.
DR   OrthoDB; 1049662at2; -.
DR   UniPathway; UPA00074; UER00133.
DR   UniPathway; UPA00074; UER00135.
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..515
FT                   /note="Bifunctional purine biosynthesis protein PurH"
FT                   /id="PRO_0000192139"
FT   DOMAIN          1..145
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
SQ   SEQUENCE   515 AA;  56511 MW;  92D3B3B63F39288A CRC64;
     MTKRALISVS DKNGIVEFAQ ELTKFGWEII STGGTKVALD QAGVTTIAID DVTGFPEMMD
     GRVKTLHPKI HGGLLARRDL DSHLQAANDH EIGLIDLVVV NLYPFKETIL RPDVTYDLAV
     ENIDIGGPSM LRSAAKNHAS VTVVVDPADY PTVLGEIAEQ GETSYATRQR LAAKVFRHTA
     AYDALIADYF TKQVGEDKPE KLTITYDLNQ PMRYGENPQQ NADFYQNALP TAYSIAAAKQ
     LNGKELSFNN IRDADAAIRI IRDFKDRPTV VALKHMNPCG IGQAETIEQA WDYAYEADPV
     SIFGGIVVLN REVDAATAEK MHPIFLEIII APGYSAEALA ILTNKKKNLR ILELAFDAQD
     ASEVEKEFTG VVGGLLVQDQ DVVVESPVDW QVVTERQPSE QEWAAMEFAW KSSKYVKSNG
     IIITNDKMTL GVGPGQTNRV ASVRIAIEQA KDRLEGAVLA SDAFFPFADN VEEIAAAGIK
     AIIQPGGSVR DQDSIDMANK YGLTMVFTGV RHFRH