ID A0A1F5ZKL5_9BACT Unreviewed; 365 AA.
AC A0A1F5ZKL5;
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=A2773_00320 {ECO:0000313|EMBL:OGG13039.1};
OS Candidatus Gottesmanbacteria bacterium RIFCSPHIGHO2_01_FULL_39_10.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798375 {ECO:0000313|EMBL:OGG13039.1, ECO:0000313|Proteomes:UP000177383};
RN [1] {ECO:0000313|EMBL:OGG13039.1, ECO:0000313|Proteomes:UP000177383}
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:OGG13039.1}.
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DR EMBL; MFJE01000063; OGG13039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5ZKL5; -.
DR STRING; 1798375.A2773_00320; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000177383; 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:OGG13039.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 46..173
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 186..349
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 365 AA; 40650 MW; 3F31D857A614D9E1 CRC64;
MSKVYSKSGV NYDLLDPIKR RAQKSGLETA VNLKNTGFNE IKKSRGESAY VLEYHDAYFV
LVEECLGTKS LVADETIKFT GKTYYDLLAQ DTVAYMVNDL ITVGARPLSI AAYWAVGSSE
WFKDKKRSSD LITGWAKACD LAGASWGGGE TPSLSGIIDK NAIDLAGACF GIVKPKQRLI
LGDKLKEGDS IIFLESRGIQ SNGVSLARKI AKQLSKGYAT LINKKLIYGE ALLIPTIIYS
KIIQDLFSEN IDIHYMSNIT GHGWRKIMRA NKQLTYSIST LPYIPEVFYF MQEKAKLSDK
DMYATFNMGA GFAIYVNPKD AEKVVIISNK NNIKAWIAGN VEKGEKQVII KPLNIVYKQQ
ELTIR
//