ID   PUR9_TRIEI              Reviewed;         517 AA.
AC   Q116T4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=Tery_1128;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RX   PubMed=25831533; DOI=10.1073/pnas.1422332112;
RA   Walworth N., Pfreundt U., Nelson W.C., Mincer T., Heidelberg J.F., Fu F.,
RA   Waterbury J.B., Glavina del Rio T., Goodwin L., Kyrpides N.C., Land M.L.,
RA   Woyke T., Hutchins D.A., Hess W.R., Webb E.A.;
RT   "Trichodesmium genome maintains abundant, widespread noncoding DNA in situ,
RT   despite oligotrophic lifestyle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:4251-4256(2015).
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; CP000393; ABG50490.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q116T4; -.
DR   SMR; Q116T4; -.
DR   STRING; 203124.Tery_1128; -.
DR   KEGG; ter:Tery_1128; -.
DR   eggNOG; COG0138; Bacteria.
DR   HOGENOM; CLU_016316_5_2_3; -.
DR   OrthoDB; 9802065at2; -.
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   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; Transferase.
FT   CHAIN           1..517
FT                   /note="Bifunctional purine biosynthesis protein PurH"
FT                   /id="PRO_1000018984"
FT   DOMAIN          1..146
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
SQ   SEQUENCE   517 AA;  56371 MW;  30B1AB24FF63B165 CRC64;
     MKRLALLSTS DKTGLIDLAK SLVTEFDYEI ISSGGTAKTL KDAGIYVTKV SDYTGFPEIL
     GGRVKTLHPR IHGGILARKD LPQDVEELNA NNIRPIDLVV VNLYPFEETI SKPEVTLAEA
     IEKIDIGGPA MLRASAKNFA HLTVLCNHFQ YNSYLEELRK NAGEVSLEFR QKCALAGFKH
     TATYDQAIAT YLQEQQTTSE SEKSEKEIFF LSGKKIKTLR YGENPHQYAT WYQRGINASG
     WGASKIIQGK ELSYNNLVDL EAARRIIIEF SDAPTVAILK HTNPCGVAVD ETILAAYERA
     FAGDSVSAFG GIVALNKSID AATAKAMTKT FLECVVAPGC EPEAEKIFKS KSKLRVLISP
     YFKQSEPETI KVISGGFLVQ DTDDTIDNYS DWKIVTEKQP TTEQIEELMF AWKVVKHVKS
     NAIVVTKNRA TVGIGAGQMN RVGAVKIALE QAGEKAIGGV LASDAFFPFD DSVKTAAAAG
     VTAIIQPGGS LKDKDSIAAA NELGLIMILT GIRHFLH
//