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Database: UniProt
Entry: A0A1I6PZU6_9SPHI
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ID   A0A1I6PZU6_9SPHI        Unreviewed;       392 AA.
AC   A0A1I6PZU6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   02-APR-2025, entry version 19.
DE   RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00020367};
DE            EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047};
DE   AltName: Full=AIR synthase {ECO:0000256|ARBA:ARBA00032931};
DE   AltName: Full=AIRS {ECO:0000256|ARBA:ARBA00033093};
DE   AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|ARBA:ARBA00031908};
GN   ORFNames=SAMN05660206_10243 {ECO:0000313|EMBL:SFS45605.1};
OS   Sphingobacterium wenxiniae.
OC   Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
OC   Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=683125 {ECO:0000313|EMBL:SFS45605.1, ECO:0000313|Proteomes:UP000198785};
RN   [1] {ECO:0000313|EMBL:SFS45605.1, ECO:0000313|Proteomes:UP000198785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22789 {ECO:0000313|EMBL:SFS45605.1,
RC   ECO:0000313|Proteomes:UP000198785};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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 + phosphate +
CC         H(+); Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, ChEBI:CHEBI:147287,
CC         ChEBI:CHEBI:456216; EC=6.3.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00049057};
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}.
CC   -!- SIMILARITY: Belongs to the AIR synthase family.
CC       {ECO:0000256|ARBA:ARBA00010280}.
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DR   EMBL; FOZZ01000002; SFS45605.1; -; Genomic_DNA.
DR   RefSeq; WP_093363614.1; NZ_FOZZ01000002.1.
DR   AlphaFoldDB; A0A1I6PZU6; -.
DR   STRING; 683125.SAMN05660206_10243; -.
DR   OrthoDB; 9802507at2; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000198785; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:TreeGrafter.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046084; P:adenine biosynthetic process; IEA:TreeGrafter.
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   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   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};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:SFS45605.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198785}.
FT   DOMAIN          46..166
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          241..381
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   392 AA;  43058 MW;  F5BF69BD63E703F8 CRC64;
     MSDLKYNQRG VSAGKEDVHN AIKNIDKGLF PKAFCKIIPD ILGGDENWCN IMHADGAGTK
     SSLAYVYWKE TGDASVWRGI AQDAIIMNID DLLCVGAIDN ILLSSTIGRN KNCIPGEVIA
     EIINGTEEIL EELRKLGIGI YSTGGETADV GDLVRTIIVD STVTCRMKRE DVISNHRIQG
     GNVIVGLASY GKANYEKEYN GGMGSNGLTS ARHDVFHKAI AEKYPESYDP AVPYELVFAG
     GCALTDKIKT ETGEEVTAGK LVLSPTRTYA PVIKAILDKY RKQIDGMVHC SGGAQTKVLH
     FVEDVHVIKD NLFPIPPLFE LIQKQSNTDW KEMYKVFNMG HRMELYVSEE IAADIIAISE
     SFGIPAQIIG RVESASQKKV TIRSPFGEFI YE
//
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