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Database: UniProt
Entry: A0A0A7V2S1_9ARCH
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ID   A0A0A7V2S1_9ARCH        Unreviewed;       340 AA.
AC   A0A0A7V2S1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
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   ECO:0000313|EMBL:AJA93123.1};
GN   ORFNames=A7X95_02875 {ECO:0000313|EMBL:PTL88222.1}, T478_1006
GN   {ECO:0000313|EMBL:AJA93123.1};
OS   Candidatus Nitrosopelagicus brevis.
OC   Archaea; Nitrososphaerota.
OX   NCBI_TaxID=1410606 {ECO:0000313|EMBL:AJA93123.1, ECO:0000313|Proteomes:UP000030944};
RN   [1] {ECO:0000313|EMBL:AJA93123.1, ECO:0000313|Proteomes:UP000030944}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN25 {ECO:0000313|EMBL:AJA93123.1}, and V2
RC   {ECO:0000313|Proteomes:UP000030944};
RX   PubMed=25587132; DOI=10.1073/pnas.1416223112;
RA   Santoro A.E., Dupont C.L., Richter R.A., Craig M.T., Carini P.,
RA   McIlvin M.R., Yang Y., Orsi W.D., Moran D.M., Saito M.A.;
RT   "Genomic and proteomic characterization of "Candidatus Nitrosopelagicus
RT   brevis": An ammonia-oxidizing archaeon from the open ocean.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:1173-1178(2015).
RN   [2] {ECO:0000313|EMBL:PTL88222.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U25 {ECO:0000313|EMBL:PTL88222.1};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000241022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U25 {ECO:0000313|Proteomes:UP000241022};
RA   Dupont C., Santoro A.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:PTL88222.1, ECO:0000313|Proteomes:UP000241022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U25 {ECO:0000313|EMBL:PTL88222.1,
RC   ECO:0000313|Proteomes:UP000241022};
RA   Carini P.;
RT   "Transcriptomics of ammonia oxidizing archaea.";
RL   Submitted (APR-2018) 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}.
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DR   EMBL; CP007026; AJA93123.1; -; Genomic_DNA.
DR   EMBL; LXWN01000001; PTL88222.1; -; Genomic_DNA.
DR   RefSeq; WP_048106957.1; NZ_LXWN01000001.1.
DR   STRING; 1410606.T478_1006; -.
DR   GeneID; 24816890; -.
DR   KEGG; nbv:T478_1006; -.
DR   HOGENOM; CLU_047116_0_0_2; -.
DR   OrthoDB; 6605at2157; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000030944; Chromosome.
DR   Proteomes; UP000241022; 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:UP000030944}.
FT   DOMAIN          44..162
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          175..332
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   340 AA;  36870 MW;  A117EF7DAE187E5F CRC64;
     MTISYKKAGV DITEIKKSQR AIGKLIGSTH NLQKMAKMTH GFGHYAGIVE IPGGKLLATH
     TDGVGTKVMI ANLMKKYDTI GIDCIAMNVN DIICIGATPI SFVDYIAANK NDQKIFKQIV
     SGLVKGAKKS SMPIVGGETA IMSDLIAGKG FGFDLAGMVV GMLSKKDMVL GDKIKPNDVI
     IGIKSSGLHS NGYSLARKAL LTKYSVKDNI KGIGNLGNAL LRPTEIYVKP VLEAVKKCKI
     HGLAHITGGS FTKLLRLKQI GYNLDSMPKT PALMQLIEDS GVKNEEMYKT FNMGIGFCII
     APENQTKNIH KIFKKHKTKS YEIGRISKNK GVFINKLKIA
//
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