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Database: UniProt
Entry: F4B9S9_ACIHW
LinkDB: F4B9S9_ACIHW
Original site: F4B9S9_ACIHW 
ID   F4B9S9_ACIHW            Unreviewed;       322 AA.
AC   F4B9S9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
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   OrderedLocusNames=Ahos_1111 {ECO:0000313|EMBL:AEE93995.1};
OS   Acidianus hospitalis (strain W1).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Acidianus.
OX   NCBI_TaxID=933801 {ECO:0000313|EMBL:AEE93995.1, ECO:0000313|Proteomes:UP000008458};
RN   [1] {ECO:0000313|EMBL:AEE93995.1, ECO:0000313|Proteomes:UP000008458}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W1 {ECO:0000313|EMBL:AEE93995.1,
RC   ECO:0000313|Proteomes:UP000008458};
RX   PubMed=21607549; DOI=10.1007/s00792-011-0379-y;
RA   You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D.,
RA   She Q., Liu S.J., Garrett R.A.;
RT   "Genomic analysis of Acidianus hospitalis W1 a host for studying
RT   crenarchaeal virus and plasmid life cycles.";
RL   Extremophiles 15:487-497(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=W1;
RA   You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D.,
RA   Liu S.J., Garrett R.A.;
RT   "Genomic analyses of Acidianus hospitalis W1 a host for studying
RT   crenarchaeal virus and plasmid life cycles.";
RL   Extremophiles 0:0-0(2011).
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; CP002535; AEE93995.1; -; Genomic_DNA.
DR   RefSeq; WP_013775911.1; NC_015518.1.
DR   AlphaFoldDB; F4B9S9; -.
DR   STRING; 933801.Ahos_1111; -.
DR   GeneID; 10600585; -.
DR   KEGG; aho:Ahos_1111; -.
DR   eggNOG; arCOG00639; Archaea.
DR   HOGENOM; CLU_047116_0_0_2; -.
DR   OMA; GCEQAGC; -.
DR   OrthoDB; 6605at2157; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000008458; 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}.
FT   DOMAIN          42..153
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          163..312
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   322 AA;  35335 MW;  891607F541FC43D0 CRC64;
     MVSEYKKAGV DLNKIKEIHE YIAKEISSTY RNVLLGAGHY SGVINYNGIK LALHTDGVGT
     KTLLALKSGI FEPVGIDCVA MNVNDLVSIG AKPLALVDYL AMEKPMDDVI KGVMNGLVKG
     AIESEAEIVG GETAIMKDVI NGFDLSCTAL GVVDEIKDGH DVKPGDVILG LRSNGIHSNG
     YSLVRKLIDD GKLSFEDWKE EIMKPTKIYV KPILSVLPMI KAAAHITGGS FSKLRRVTNY
     HIELKMPEPQ DIFKEIEKAG VSHEEMYKVF NMGIGMVVFT SPEYKDDVIK NIQKFVEVYE
     IGKVSEGSGI TIFTYKNAVL YL
//
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