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Database: UniProt
Entry: I9ET19_9BACE
LinkDB: I9ET19_9BACE
Original site: I9ET19_9BACE 
ID   I9ET19_9BACE            Unreviewed;       388 AA.
AC   I9ET19;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00020367};
DE            EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047};
DE   AltName: Full=AIR synthase {ECO:0000256|ARBA:ARBA00032931};
DE   AltName: Full=AIRS {ECO:0000256|ARBA:ARBA00033093};
DE   AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|ARBA:ARBA00031908};
GN   ORFNames=HMPREF1061_00261 {ECO:0000313|EMBL:EIY23529.1};
OS   Bacteroides caccae CL03T12C61.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=997873 {ECO:0000313|EMBL:EIY23529.1, ECO:0000313|Proteomes:UP000002965};
RN   [1] {ECO:0000313|EMBL:EIY23529.1, ECO:0000313|Proteomes:UP000002965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL03T12C61 {ECO:0000313|EMBL:EIY23529.1,
RC   ECO:0000313|Proteomes:UP000002965};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA   Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bacteroides caccae CL03T12C61.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP
CC         = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) +
CC         phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981,
CC         ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00023392};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC       phospho-D-ribosyl)glycinamide: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004686}.
CC   -!- SIMILARITY: Belongs to the AIR synthase family.
CC       {ECO:0000256|ARBA:ARBA00010280}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIY23529.1}.
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DR   EMBL; AGXF01000001; EIY23529.1; -; Genomic_DNA.
DR   RefSeq; WP_005679956.1; NZ_JH724079.1.
DR   AlphaFoldDB; I9ET19; -.
DR   GeneID; 75112952; -.
DR   PATRIC; fig|997873.3.peg.273; -.
DR   HOGENOM; CLU_719355_0_0_10; -.
DR   OrthoDB; 9802507at2; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000002965; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR016188; PurM-like_N.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   InterPro; IPR004733; PurM_cligase.
DR   PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1.
DR   PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          46..166
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          179..379
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   388 AA;  42326 MW;  952953E22DFEA546 CRC64;
     MSNQRYMMRG VSASKEDVHN AIKNIDKGIF PKAFCKIIPD ILGGDPDYCN IMHADGAGTK
     SSLAYMYWKE TGDLSVWKGI AQDALIMNID DLLCVGAVDN ILVSSTIGRN KLLIPGEVIS
     AIINGTDELL AELREMGVGV YATGGETADV GDLVRTIIVD STVTCRMKRS DVINNANIRP
     GDVIVGLASY GQATYEKEYN GGMGSNGLTS ARHDVFGKYL AEKYPESYDA AVPEELVYSG
     GLKLTDSVEG SPIDAGKLVL SPTRTYAPVV KKLLDALRSE IHGMVHCSGG AQTKVLHFVE
     NVRVVKDNLF PVPPLFKTIQ EQSGTDWAEM YKVFNMGHRL EVYLSPEHAE EVIAISESFG
     IPAQIVGRIE ACEQTELIIK SEFGEFRY
//
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