ID A0A063BF96_9BURK Unreviewed; 351 AA.
AC A0A063BF96;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
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 ORFNames=LIG30_1833 {ECO:0000313|EMBL:KDB09081.1};
OS Burkholderia sp. lig30.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1192124 {ECO:0000313|EMBL:KDB09081.1, ECO:0000313|Proteomes:UP000027020};
RN [1] {ECO:0000313|EMBL:KDB09081.1, ECO:0000313|Proteomes:UP000027020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LIG30 {ECO:0000313|Proteomes:UP000027020};
RA Woo H.L., Utturkar S.M., Klingeman D.M., Simmons B.A., DeAngelis K.M.,
RA Brown S.D., Hazen T.C.;
RT "Draft Genome of the Lignin-degrading Burkholderia sp. Strain LIG30,
RT Isolated from Wet Tropical Forest Soil.";
RL Submitted (MAR-2014) 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}.
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:KDB09081.1}.
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DR EMBL; JGVW01000061; KDB09081.1; -; Genomic_DNA.
DR RefSeq; WP_038711041.1; NZ_JGVW01000061.1.
DR AlphaFoldDB; A0A063BF96; -.
DR STRING; 1192124.LIG30_1833; -.
DR PATRIC; fig|1192124.4.peg.1608; -.
DR eggNOG; COG0150; Bacteria.
DR OrthoDB; 9777881at2; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000027020; Unassembled WGS sequence.
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:UP000027020}.
FT DOMAIN 65..170
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 183..346
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 351 AA; 36996 MW; E3FEB98CC755B15E CRC64;
MNPPKTAPDA QGLSYRDAGV DIDAGDALVD KIKPFAKKTL RDGVLGGIGG FGALFEVPKK
YREPVLVSGT DGVGTKLKLA FHLNKHDTVG QDLVAMSVND ILVQGAEPLF FLDYFACGKL
DVETAATVVK GIATGCELAG CALIGGETAE MPGMYPDGEY DLAGFAVGAV EKSKIIDGST
IAEGDVVLGL ASSGIHSNGF SLVRKIIERA NPDLSADFHG RSLADTLMAP TRIYVKPLLA
MMEKIAVKGM AHITGGGLVE NIPRVLREGL TAELDKNAWP LPPLFQWLQE HGGVADAEMH
RVFNCGIGMA VIVAAADADE ALRQLTDAGE QVWKIGTVRA SREGEAQTVV V
//
