ID A0A2P7TEY6_9SPHI Unreviewed; 362 AA.
AC A0A2P7TEY6;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=C7N43_29970 {ECO:0000313|EMBL:PSJ73279.1};
OS Sphingobacteriales bacterium UPWRP_1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=2116516 {ECO:0000313|EMBL:PSJ73279.1, ECO:0000313|Proteomes:UP000240367};
RN [1] {ECO:0000313|EMBL:PSJ73279.1, ECO:0000313|Proteomes:UP000240367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPWRP_1 {ECO:0000313|EMBL:PSJ73279.1,
RC ECO:0000313|Proteomes:UP000240367};
RA Tan S.M.;
RT "Obtaining draft genomes of rare unknown microbial groups and defining 1
RT their spatial structures from highly complex communities.";
RL Submitted (MAR-2018) 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:PSJ73279.1}.
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DR EMBL; PXYE01000177; PSJ73279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7TEY6; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000240367; 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:PSJ73279.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000240367}.
FT DOMAIN 53..150
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 180..348
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 362 AA; 39308 MW; 03AF9E4711618D4B CRC64;
MQNKQSGFDI DLGNQCSQNA FSWAKKTFAN RAGKAGQVVL KVDGAFSNML DFNGVKIGIT
SDGIGTKIEV AERTGIYDTL GYDLVAMVAD DLIAGGFVPT NISNIIDVDN LDYNIIDQLM
RGLHHAANFA GIAVTGGEIA ELGSRISGWG NNMHFNWCST AIGVLHPRLQ HPVDGSAVHE
GDAVIALRSR GFRSNGFSAV RKIMQEQFGN QWHTQPYSDG QSWGEILLTP SLIFAPAVTN
VINEGIGIKG IAHITGGGIA DNFRRVLKVN RMGANLHNLF EPHPFMVQLA NYGHVTPQQA
YLYWNMGNGM LLITANKDAE KTVELLNTAG EYQAQVAGHI TAKRRITIET VWGSIITALE
NE
//
