ID G8LQS4_9FLAO Unreviewed; 328 AA.
AC G8LQS4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
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:AEU09492.1};
GN ORFNames=BLBCPU_451 {ECO:0000313|EMBL:AEU09492.1};
OS Blattabacterium sp. (Cryptocercus punctulatus) str. Cpu.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=1075399 {ECO:0000313|EMBL:AEU09492.1, ECO:0000313|Proteomes:UP000007112};
RN [1] {ECO:0000313|EMBL:AEU09492.1, ECO:0000313|Proteomes:UP000007112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cpu {ECO:0000313|EMBL:AEU09492.1,
RC ECO:0000313|Proteomes:UP000007112};
RX PubMed=22094859;
RA Neef A., Latorre A., Pereto J., Silva F.J., Pignatelli M., Moya A.;
RT "Genome economization in the endosymbiont of the wood roach Cryptocercus
RT punctulatus due to drastic loss of amino acid synthesis capabilities.";
RL Genome Biol. Evol. 3:1437-1448(2011).
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; CP003015; AEU09492.1; -; Genomic_DNA.
DR RefSeq; WP_014246380.1; NC_016621.1.
DR AlphaFoldDB; G8LQS4; -.
DR STRING; 1075399.BLBCPU_451; -.
DR KEGG; bcp:BLBCPU_451; -.
DR eggNOG; COG0150; Bacteria.
DR HOGENOM; CLU_047116_0_0_10; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000007112; 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}.
FT DOMAIN 45..150
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 163..322
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 328 AA; 36838 MW; AE201493C1D68F34 CRC64;
MKESNRTIYK ISPILEKTYN NKVIGSLDNF AALYKMPSSE YKEPVLVSGV DGVGTKLLLA
INYQKYDVIG EDCFAMCAND ILCHGAKPLF FLDYLACGKL DSNIAEKIIQ GIATSCKKTN
TCLIGGEIAE IPSIYKKKDY DIAGFCVGIV EKKKVIDGKK TIKEGDILIG IPSSGVHSNG
FSLIRNIFYT EDLLMKKFQK KPFYETLLIP TRIYYSTIQI LLKEFVIHGL VHVTGGGIYD
NLFRVLPENL LAIVDKKKIP ILPIFNHIQE KGFLSDQKMW HTFNMGVGMI IIVSIKDQGP
IFDRLRFLGE NPFVFGNIVK GDKKVFLK
//
