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Database: UniProt
Entry: A0A1Y3AA45_9EURY
LinkDB: A0A1Y3AA45_9EURY
Original site: A0A1Y3AA45_9EURY 
ID   A0A1Y3AA45_9EURY        Unreviewed;       348 AA.
AC   A0A1Y3AA45;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00013047, 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|HAMAP-Rule:MF_00741};
DE   AltName: Full=AIRS {ECO:0000256|HAMAP-Rule:MF_00741};
DE   AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|HAMAP-Rule:MF_00741};
GN   Name=purM {ECO:0000256|HAMAP-Rule:MF_00741};
GN   ORFNames=B9G49_05420 {ECO:0000313|EMBL:OTF00859.1};
OS   Halorubrum sp. SD683.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=1855873 {ECO:0000313|EMBL:OTF00859.1, ECO:0000313|Proteomes:UP000194293};
RN   [1] {ECO:0000313|EMBL:OTF00859.1, ECO:0000313|Proteomes:UP000194293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD683 {ECO:0000313|EMBL:OTF00859.1,
RC   ECO:0000313|Proteomes:UP000194293};
RA   De La Haba R., Sanchez-Porro C., Infante-Dominguez C., Corral P.,
RA   Ventosa A.;
RT   "MLSA of the genus Halorubrum.";
RL   Submitted (MAY-2017) 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|HAMAP-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. {ECO:0000256|HAMAP-
CC       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:OTF00859.1}.
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DR   EMBL; NEWJ01000012; OTF00859.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3AA45; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000194293; 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}.
FT   DOMAIN          53..166
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          178..330
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   348 AA;  35530 MW;  11AB542760377C59 CRC64;
     MTEGDGSGGG GPDGDDELTY ADAGVDIDAS EAATAALIGA VGSDSDADGS GSDYAGLLDI
     GDRYLALATD GVGTKLLVAE ALGDYSTVGI DCIAMNVNDL VAAGVRPVAF VDYLAVDEPD
     ERFAEQVGEG LARGAELADI ELVGGETAVM PDVVRGLDLA GTCAGLAAKD GVFDGRAEPG
     DALVGWRSSG IHSNGLTLAR EAVTRDHAYA DPCPFGDYET LGNALLEPTA IYTDLLDPMR
     DHGVRGAAHV TGGGWTNLDR LGDHRYVVDD AFDSQPVFEF VRSEGNVSDE EMYRTFNMGT
     GFVAAVDADA ADALADATDG RVIGRVEDGA ADAGGDGGAS VAIRGLEL
//
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