ID I0TCH3_9BACT Unreviewed; 382 AA.
AC I0TCH3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=HMPREF9969_2226 {ECO:0000313|EMBL:EID33326.1};
OS Prevotella sp. oral taxon 306 str. F0472.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1095752 {ECO:0000313|EMBL:EID33326.1, ECO:0000313|Proteomes:UP000004421};
RN [1] {ECO:0000313|EMBL:EID33326.1, ECO:0000313|Proteomes:UP000004421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0472 {ECO:0000313|EMBL:EID33326.1,
RC ECO:0000313|Proteomes:UP000004421};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (MAR-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:EID33326.1}.
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DR EMBL; AJIN01000042; EID33326.1; -; Genomic_DNA.
DR AlphaFoldDB; I0TCH3; -.
DR STRING; 1095752.HMPREF9969_2226; -.
DR PATRIC; fig|1095752.3.peg.1374; -.
DR eggNOG; COG0150; Bacteria.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000004421; 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 40..160
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 173..369
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 382 AA; 42013 MW; DC2D5CCED8480AC5 CRC64;
MMRGVSAAKE DVHNAIKNID KGLYPQAFCK IIPDILGGDP EYCNIMHADG AGTKSSLAYM
YWKETGDLSV WHGIAQDAIV MNTDDLLCVG AVDNILVSST IGRNKMLVPG EVISAIINGT
DELLADMRKM GIGIYPTGGE TADVGDLVRT IIVDSTVTCR MRRKDVIDNA NIRPGDVIVG
LSSTGQATYE TRYNGGMGSN GLTSARHDVF AKYLAENYPE SYDHAVPEEL VYSGKYKLTD
SVEGSPVNAG ELVLSPTRTY APVIKRLLDE LRPEVHGMVH CTGGAQTKVL HFVGENCRVI
KDNMFPVPPL FRAIKDCSGT DWKEMYQVFN MGHRMEIYVR PEVAEQVIAI SKFFNIDAQV
IGHIEEGKRS LTIKSEFGTF EY
//
