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Database: UniProt
Entry: A0A221MH89_9BACI
LinkDB: A0A221MH89_9BACI
Original site: A0A221MH89_9BACI 
ID   A0A221MH89_9BACI        Unreviewed;       340 AA.
AC   A0A221MH89;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=CFK40_19295 {ECO:0000313|EMBL:ASN07004.1};
OS   Virgibacillus necropolis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN07004.1, ECO:0000313|Proteomes:UP000204391};
RN   [1] {ECO:0000313|EMBL:ASN07004.1, ECO:0000313|Proteomes:UP000204391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN07004.1,
RC   ECO:0000313|Proteomes:UP000204391};
RX   PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA   Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA   Rodriguez-Diaz M., Swings J., De Vos P.;
RT   "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov. and
RT   Virgibacillus picturae sp. nov., three novel species isolated from
RT   deteriorated mural paintings, transfer of the species of the genus
RT   salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov. and
RT   Virgibacillus salexigens comb. nov., and emended description of the genus
RT   Virgibacillus.";
RL   Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
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; CP022437; ASN07004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A221MH89; -.
DR   KEGG; vne:CFK40_19295; -.
DR   OrthoDB; 9802507at2; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000204391; 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:UP000204391}.
FT   DOMAIN          56..161
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          173..336
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   340 AA;  36091 MW;  6D02455562FE7F86 CRC64;
     MSDAYREAGV DVEKGYQAVD LMKKHIAKTN RKEVLGGVGG FAGLFDLSGF SYKEPVLVSG
     TDGVGTKLKL AFQLDKHDSI GKDLVAMCVN DIIAQGAQAL FFLDYIACGK NNPEMIEQIV
     AGVADGCVDA GAALIGGETA EMPGMYQDNE YDVAGFAVGI AEKSKLISGE HIQAGDVVIG
     LPSSGIHSNG YSLVRKIVAE LDLADSYQGL SKSLGATLLE PTKIYAKPIN KLTQTVDVKG
     ISHITGGGFY ENIPRMLPAG LGVEVDRASW NVPEIFTFLQ KQGNVSDYDM FGVFNMGIGM
     AVVIDQDKAD LAIDLLQENG EAAVVIGTVS EHEGVRFTND
//
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