ID I0I2E3_CALAS Unreviewed; 329 AA.
AC I0I2E3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00020367, ECO:0000256|HAMAP-Rule:MF_00741};
DE EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047, ECO:0000256|HAMAP-Rule:MF_00741};
DE AltName: Full=AIR synthase {ECO:0000256|ARBA:ARBA00032931, ECO:0000256|HAMAP-Rule:MF_00741};
DE AltName: Full=AIRS {ECO:0000256|ARBA:ARBA00033093, ECO:0000256|HAMAP-Rule:MF_00741};
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|ARBA:ARBA00031908, ECO:0000256|HAMAP-Rule:MF_00741};
GN Name=purM {ECO:0000256|HAMAP-Rule:MF_00741,
GN ECO:0000313|EMBL:BAL99430.1};
GN OrderedLocusNames=CLDAP_13910 {ECO:0000313|EMBL:BAL99430.1};
OS Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS STL-6-O1).
OC Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC Caldilinea.
OX NCBI_TaxID=926550 {ECO:0000313|EMBL:BAL99430.1, ECO:0000313|Proteomes:UP000007880};
RN [1] {ECO:0000313|EMBL:BAL99430.1, ECO:0000313|Proteomes:UP000007880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC {ECO:0000313|Proteomes:UP000007880};
RA Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Hanada S., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT 102666).";
RL Submitted (FEB-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, ECO:0000256|HAMAP-
CC Rule:MF_00741};
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, ECO:0000256|HAMAP-Rule:MF_00741}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00741}.
CC -!- SIMILARITY: Belongs to the AIR synthase family.
CC {ECO:0000256|ARBA:ARBA00010280, ECO:0000256|HAMAP-Rule:MF_00741}.
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DR EMBL; AP012337; BAL99430.1; -; Genomic_DNA.
DR AlphaFoldDB; I0I2E3; -.
DR STRING; 926550.CLDAP_13910; -.
DR KEGG; cap:CLDAP_13910; -.
DR PATRIC; fig|926550.5.peg.1469; -.
DR eggNOG; COG0150; Bacteria.
DR HOGENOM; CLU_047116_0_0_0; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000007880; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02196; PurM; 1.
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 HAMAP; MF_00741; AIRS; 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 NCBIfam; TIGR00878; purM; 1.
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, ECO:0000256|HAMAP-
KW Rule:MF_00741}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00741};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00741};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00741}; Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007880}.
FT DOMAIN 43..151
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 164..323
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 329 AA; 34612 MW; 081FBF8298F4E1F9 CRC64;
MDIDAGAAAV SAMKAAIRST FTTNVLADVG SFGGVFALDN LPAQPVLVAS IDGVGTKVKL
AAEFGRWRSI GHDLVNHCVN DILVQNARPL FFLDYLATSR LDPAVAAEVV TGIAEACRAV
GCALIGGETA EMPGVYAEGA VDVAGAIVGL VGREHLLPKP ETMEAGDALI GLASSGPHTN
GYSLIRKIIA GRALFDPLPD GSTLIDALLA PHRCYLSHVE AIQRAGYPIK GMAHITGGGL
LDNLPRILPA HLTARVVARS WERPPIFDQL VHWGELDLIE AHRVFNMGIG MVLVTPAAAA
EPILNILSDA VVIGRLVERQ DEQAVKLIV
//
