ID I5CAB2_9BACT Unreviewed; 388 AA.
AC I5CAB2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=A3SI_01851 {ECO:0000313|EMBL:EIM78764.1};
OS Nitritalea halalkaliphila LW7.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Nitritalea.
OX NCBI_TaxID=1189621 {ECO:0000313|EMBL:EIM78764.1, ECO:0000313|Proteomes:UP000005551};
RN [1] {ECO:0000313|EMBL:EIM78764.1, ECO:0000313|Proteomes:UP000005551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LW7 {ECO:0000313|EMBL:EIM78764.1,
RC ECO:0000313|Proteomes:UP000005551};
RA Jangir P.K., Singh A., Shivaji S., Sharma R.;
RT "Genome sequence of Nitritalea halalkaliphila LW7.";
RL Submitted (MAY-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:EIM78764.1}.
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DR EMBL; AJYA01000002; EIM78764.1; -; Genomic_DNA.
DR RefSeq; WP_009053313.1; NZ_AJYA01000002.1.
DR AlphaFoldDB; I5CAB2; -.
DR STRING; 1189621.A3SI_01851; -.
DR PATRIC; fig|1189621.3.peg.388; -.
DR OrthoDB; 9802507at2; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000005551; 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:EIM78764.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005551}.
FT DOMAIN 45..165
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 179..379
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 388 AA; 42432 MW; 5D79BE384D7B09F8 CRC64;
MNERYMQRGV SAAKEDVHRA ISGLDKGLFP KAFCKIVPDV LGGDPDYCNI MHADGAGTKS
SLAYLYWKET GDLSVWKGIA QDAIIMNIDD LLCVGAVDNI LVSSTIGRNK HLIPGEVIEA
LIQGTEEVLQ MLRAHGVQVL LTGGETADVG DLVRTVIVDS TVTCRMKRAD VISNDRIAAG
SVIVGLASYG QADYETQYNG GMGSNGLTSA RHDVFHHGLA AKYPESFDPS VSEDLVYTGS
FRLTDPLEEL GVDVGQLVLS PTRTYAPVMV EVLKQFRSQI QGIVHCSGGA QTKVLHFIEG
LHVIKDHLFP TPPLFKIIQE ESGTDWQEMY KVFNMGHRLE LYVPEEIAGE IIRISQSFGI
EAQVIGRVEA APVKQVTVKG EHGTYHYF
//
