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Database: UniProt
Entry: D9XUE8_9ACTN
LinkDB: D9XUE8_9ACTN
Original site: D9XUE8_9ACTN 
ID   D9XUE8_9ACTN            Unreviewed;       520 AA.
AC   D9XUE8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=Bifunctional purine biosynthesis protein PurH {ECO:0000256|HAMAP-Rule:MF_00139};
DE   Includes:
DE     RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_00139};
DE              EC=2.1.2.3 {ECO:0000256|HAMAP-Rule:MF_00139};
DE     AltName: Full=AICAR transformylase {ECO:0000256|HAMAP-Rule:MF_00139};
DE   Includes:
DE     RecName: Full=IMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_00139};
DE              EC=3.5.4.10 {ECO:0000256|HAMAP-Rule:MF_00139};
DE     AltName: Full=ATIC {ECO:0000256|HAMAP-Rule:MF_00139};
DE     AltName: Full=IMP synthase {ECO:0000256|HAMAP-Rule:MF_00139};
DE     AltName: Full=Inosinicase {ECO:0000256|HAMAP-Rule:MF_00139};
GN   Name=purH {ECO:0000256|HAMAP-Rule:MF_00139};
GN   ORFNames=SSRG_02398 {ECO:0000313|EMBL:EFL39594.1};
OS   Streptomyces griseoflavus Tu4000.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL39594.1, ECO:0000313|Proteomes:UP000002968};
RN   [1] {ECO:0000313|EMBL:EFL39594.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu4000 {ECO:0000313|EMBL:EFL39594.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|ARBA:ARBA00004954, ECO:0000256|HAMAP-
CC       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:0000256|ARBA:ARBA00004844, ECO:0000256|HAMAP-Rule:MF_00139}.
CC   -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC       region. {ECO:0000256|HAMAP-Rule:MF_00139}.
CC   -!- SIMILARITY: Belongs to the PurH family. {ECO:0000256|ARBA:ARBA00007667,
CC       ECO:0000256|HAMAP-Rule:MF_00139}.
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DR   EMBL; GG657758; EFL39594.1; -; Genomic_DNA.
DR   RefSeq; WP_004926844.1; NZ_GG657758.1.
DR   AlphaFoldDB; D9XUE8; -.
DR   STRING; 467200.SSRG_02398; -.
DR   eggNOG; COG0138; Bacteria.
DR   HOGENOM; CLU_016316_5_2_11; -.
DR   OrthoDB; 9802065at2; -.
DR   UniPathway; UPA00074; UER00133.
DR   Proteomes; UP000002968; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00139};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_00139};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_00139};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00139}.
FT   DOMAIN          1..152
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
SQ   SEQUENCE   520 AA;  54782 MW;  74373F4AAB45FD50 CRC64;
     MTAESNKRAI RRALVSVYDK TGLEDLARGL HEAGVELVST GSTAARIAAA GVPVTKVEEL
     TGFPECLDGR VKTLHPKVHA GILADLRLED HRNQLAELGV EPFDLVVVNL YPFRETVASG
     ATPDECVEQI DIGGPSMVRA AAKNHPSVAV VTSPARYADV LGAVRDGGFD LTTRKRLAAE
     AFRHTAAYDV AVASWFASDY APVDDSGFPD FLGATWERKN TLRYGENPHQ PAALYVSGTG
     GLAEAEQLHG KEMSYNNYTD TDAALRAAYD HAGPAVAIIK HANPCGIATG ADVAEAHRKA
     HACDPLSAFG GVIAVNRPVS KEMAEQVAEI FTEVIVAPDY EDGALEALTK KKNIRVLRAP
     GAPSAPVEVK PVDGGALLQV TDRLQAEGDD PAAWTLATGA ALSEAELADL AFAWKACRAV
     KSNAILLAKD GASVGVGMGQ VNRVDSAKLA VERAGAERAA GSFAASDAFF PFPDGLEILV
     EAGVRAVVQP GGSVRDELVV EAAKKAGVTM YFTGTRHFFH
//
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