ID A0A2G0CJ78_9BACT Unreviewed; 392 AA.
AC A0A2G0CJ78;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
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=CGL56_02970 {ECO:0000313|EMBL:PHL00022.1};
OS Neolewinella marina.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC Neolewinella.
OX NCBI_TaxID=438751 {ECO:0000313|EMBL:PHL00022.1, ECO:0000313|Proteomes:UP000226437};
RN [1] {ECO:0000313|EMBL:PHL00022.1, ECO:0000313|Proteomes:UP000226437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MKG-38 {ECO:0000313|EMBL:PHL00022.1,
RC ECO:0000313|Proteomes:UP000226437};
RA Wang K.;
RT "The draft genome sequence of Lewinella marina KCTC 32374.";
RL Submitted (OCT-2017) 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:PHL00022.1}.
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DR EMBL; PDLO01000001; PHL00022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G0CJ78; -.
DR OrthoDB; 9802507at2; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000226437; 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:PHL00022.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000226437}.
FT DOMAIN 45..161
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 177..376
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 392 AA; 42788 MW; 02B22996D37B7D87 CRC64;
MSTKYEQRGV SATKSEVHDA IQGLDKGLYP KAFCKVLPDI AGGDPEYCNV MHADTAGTKT
SLAYLYWKET GDLSVWEGIV QDSLVMNLDD MGCVGAVDNI LISSTIGRNK NRIPGEVLKT
IIQGAQKFAD RMAEQGVGLH LTGGETADVG DIVRTIDVGY TTFARLRRDE VIVNDIRPGN
VIVGLASYGQ ATYEDEYNGG MGSNGLTSAR HDVFRKEYAD KYPESFDPEV PREVVYTGSR
ALTDKITVDG VETTVGKLVL SPTRTYLPVL KKLLQEVGPG LSGLIHCTGG AQTKVVKFID
PDVRVVKDKL FPAPPLFDLI RQESGTDWRE MYQVFNMGHR LEAYVGERDA QTVIDLARSF
GIDARIIGHV EAGGEQASVR LTTPGGVEEY TD
//
