ID A0A1F5GVN2_9BACT Unreviewed; 374 AA.
AC A0A1F5GVN2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=A3F02_01720 {ECO:0000313|EMBL:OGD95943.1};
OS Candidatus Curtissbacteria bacterium RIFCSPHIGHO2_12_FULL_38_9b.
OC Bacteria; Candidatus Curtissbacteria.
OX NCBI_TaxID=1797720 {ECO:0000313|EMBL:OGD95943.1, ECO:0000313|Proteomes:UP000176666};
RN [1] {ECO:0000313|EMBL:OGD95943.1, ECO:0000313|Proteomes:UP000176666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGD95943.1}.
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DR EMBL; MFBJ01000039; OGD95943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5GVN2; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000176666; 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 94..182
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 196..358
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 374 AA; 41691 MW; 58CD63E315ECCA1A CRC64;
MKKNNKITYA QVGDNYLIKD PVNKLSQQAA KSTGINLKKA GFNEIQATRG ESAFVWKQGP
FLMASVIECL GTKSLVADEM RKIADPEQSR RTYYDVIANN TVATFINDLS SVGAKPLVVH
AYWAFGDNDW LEDKKRLRDF IKGWKQACDE SGATWGGGET ATLKGILNPD ACDLAGSVVG
IIKNPKNLVI DKKLRTGDRI IFVKSNGVNA NGISLARSIA KKLPQGYVTK MPNGALYGEA
ILTKSNLYAK LIQSLIQAEI DIHYITHITG HGLRKIMRGR QNFTYVIEKL FQPQEVFKFI
QKHAGLNDYE AYETYNMGQD YAIFLPAKDV KKAEAIIKKN GFESLDAGYL KKGPRQVVIK
PKNVIYFANT LDIR
//
