ID A0A1B9Y303_9FLAO Unreviewed; 392 AA.
AC A0A1B9Y303;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=BA195_05725 {ECO:0000313|EMBL:OCK44183.1};
OS Tenacibaculum soleae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=447689 {ECO:0000313|EMBL:OCK44183.1, ECO:0000313|Proteomes:UP000093186};
RN [1] {ECO:0000313|EMBL:OCK44183.1, ECO:0000313|Proteomes:UP000093186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-KL19 {ECO:0000313|EMBL:OCK44183.1,
RC ECO:0000313|Proteomes:UP000093186};
RA Eisen J.A., Coil D.A., Lujan K.M.;
RT "Draft Genome Sequence of Tenacibaculum soleae UCD-KL19.";
RL Submitted (JUN-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};
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:OCK44183.1}.
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DR EMBL; MAKX01000001; OCK44183.1; -; Genomic_DNA.
DR RefSeq; WP_068703310.1; NZ_MAKX01000001.1.
DR AlphaFoldDB; A0A1B9Y303; -.
DR STRING; 447689.BA195_05725; -.
DR OrthoDB; 9802507at2; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000093186; 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, ECO:0000313|EMBL:OCK44183.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000093186}.
FT DOMAIN 48..169
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 182..382
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 392 AA; 42942 MW; 1D503EACDA6BBA22 CRC64;
MSNEVSKRYA QRGVSASKED VHNAIKNIDK GLFPKAFCKI VPDYLTNDND YCLIMHADGA
GTKSSLAYMY WKETGDISVW KGIAQDALIM NIDDLLCVGA TDNIMLSSTI GRNKSKIPGE
VLSAIINGTE ELIEDLKGFG VTIHSTGGET ADVGDLVRTI IVDSTVTARM KRSDVIDNAN
IKAGDVIVGL ESFGQATYET EYNGGMGSNG LTSARHDVFD NYLASKYPES FDAAVPADLV
YSGNTKLTDE VENSPIDAGK LVLSPTRTYA PIIKEILSKF SSDDVHGMIH CSGGAQTKIL
HFVDELHIVK DNMFPIPPLF KLIQEQSKTD WKEMYQVFNC GHRMELYVSP EVAEDIIAIS
KSYNVNAQIV GRVAASETKK LTINSEFGTF EY
//
