ID A5EXP2_DICNV Unreviewed; 331 AA.
AC A5EXP2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00020367, ECO:0000256|HAMAP-Rule:MF_00741};
DE EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047, ECO:0000256|HAMAP-Rule:MF_00741};
DE AltName: Full=AIR synthase {ECO:0000256|ARBA:ARBA00032931, ECO:0000256|HAMAP-Rule:MF_00741};
DE AltName: Full=AIRS {ECO:0000256|ARBA:ARBA00033093, ECO:0000256|HAMAP-Rule:MF_00741};
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|ARBA:ARBA00031908, ECO:0000256|HAMAP-Rule:MF_00741};
GN Name=purM {ECO:0000256|HAMAP-Rule:MF_00741,
GN ECO:0000313|EMBL:ABQ13811.1};
GN OrderedLocusNames=DNO_1113 {ECO:0000313|EMBL:ABQ13811.1};
OS Dichelobacter nodosus (strain VCS1703A).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Dichelobacter.
OX NCBI_TaxID=246195 {ECO:0000313|EMBL:ABQ13811.1, ECO:0000313|Proteomes:UP000000248};
RN [1] {ECO:0000313|EMBL:ABQ13811.1, ECO:0000313|Proteomes:UP000000248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VCS1703A {ECO:0000313|EMBL:ABQ13811.1,
RC ECO:0000313|Proteomes:UP000000248};
RX PubMed=17468768; DOI=10.1038/nbt1302;
RA Myers G.S., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA Songer J.G., Rood J.I., Paulsen I.T.;
RT "Genome sequence and identification of candidate vaccine antigens from the
RT animal pathogen Dichelobacter nodosus.";
RL Nat. Biotechnol. 25:569-575(2007).
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, ECO:0000256|HAMAP-
CC Rule:MF_00741};
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, ECO:0000256|HAMAP-Rule:MF_00741}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00741}.
CC -!- SIMILARITY: Belongs to the AIR synthase family.
CC {ECO:0000256|ARBA:ARBA00010280, ECO:0000256|HAMAP-Rule:MF_00741}.
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DR EMBL; CP000513; ABQ13811.1; -; Genomic_DNA.
DR RefSeq; WP_012031417.1; NC_009446.1.
DR AlphaFoldDB; A5EXP2; -.
DR STRING; 246195.DNO_1113; -.
DR KEGG; dno:DNO_1113; -.
DR eggNOG; COG0150; Bacteria.
DR HOGENOM; CLU_047116_0_0_6; -.
DR OrthoDB; 9777881at2; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000000248; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02196; PurM; 1.
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 HAMAP; MF_00741; AIRS; 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 NCBIfam; TIGR00878; purM; 1.
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, ECO:0000256|HAMAP-
KW Rule:MF_00741}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00741};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00741};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00741}; Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000248}.
FT DOMAIN 54..159
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 172..324
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 331 AA; 35389 MW; E9C09F698E7913C1 CRC64;
MSLDYKSAGV DKEAGYDTVR RIKDYAAATH NARVLSQIGA FGAFYDLSGY REPVLVSGTD
GVGTKLKIAF SLEKYDTIGI DAVAMCVNDI LCHGARPQFF LDYLACGKLD SQVAAEIVKG
VAHGCQQAGA ALIGGETAEM PDFYALGEYD IAGFAVGVVE KSALIDGSKV RADDVLIGLP
SSGFHSNGYS LLRKIFTDFS KPYQETTIGA QLLTPTRIYV RPVLSVLEKH AVCGMAHITG
GGLIENIPRA YAAGLTAVID TKTLPTLPLM ELVTQHVSYE ECLGTFNMGI GFVLIVPPDE
ADAVLKTLHA QQENARIIGT MATGEEPLRF I
//
