ID A0A1G6XKI7_PEPNI Unreviewed; 345 AA.
AC A0A1G6XKI7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ORFNames=SAMN04489866_10712 {ECO:0000313|EMBL:SDD78581.1};
OS Peptococcus niger.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Peptococcus.
OX NCBI_TaxID=2741 {ECO:0000313|EMBL:SDD78581.1, ECO:0000313|Proteomes:UP000198995};
RN [1] {ECO:0000313|EMBL:SDD78581.1, ECO:0000313|Proteomes:UP000198995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20475 {ECO:0000313|EMBL:SDD78581.1,
RC ECO:0000313|Proteomes:UP000198995};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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, 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; FNAF01000007; SDD78581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6XKI7; -.
DR STRING; 2741.SAMN04489866_10712; -.
DR OrthoDB; 9802507at2; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000198995; Unassembled WGS sequence.
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:UP000198995}.
FT DOMAIN 57..162
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 175..344
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 345 AA; 36894 MW; C8E2836A274AA32C CRC64;
MKDAMTYRDA GVDISKGNEA VDKIKPLVAR TKRPEVLGGL GGFGGLFRVP EGYKKPVLVS
GTDGIGTKLK VAFMCGKHDT VGIDAVAMCV NDILVAGAEP LFFLDYVAVG KLNPDQLAEV
VAGIAEGCVQ SGCALIGGET AEMPGFYQND EYDVAGFSVG IVEEDRLLDG SAVGEGDVIL
GLPSTGLHSN GYSLARKIAF ERAGKQTDSY IEELGERLGE ALLRPTRIYV KDVLPILKEK
PGVIHAMAHI TGGGLVENVP RVLPEGLSAE IKTEAWPRLP IFDWLAKEGQ VPEEDMWRTF
NMGIGLVLVI GAADAQAVCE DFQARDIAYY DIGRIVKGDQ SVVRV
//
