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Database: UniProt
Entry: W1SRJ2_9BACI
LinkDB: W1SRJ2_9BACI
Original site: W1SRJ2_9BACI 
ID   W1SRJ2_9BACI            Unreviewed;       344 AA.
AC   W1SRJ2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=BAVI_01320 {ECO:0000313|EMBL:ETI70664.1};
OS   Neobacillus vireti LMG 21834.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI70664.1, ECO:0000313|Proteomes:UP000018877};
RN   [1] {ECO:0000313|EMBL:ETI70664.1, ECO:0000313|Proteomes:UP000018877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI70664.1,
RC   ECO:0000313|Proteomes:UP000018877};
RX   PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA   Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT   "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT   potent source and sink for nitric and nitrous oxide under high nitrate
RT   conditions.";
RL   Environ. Microbiol. 16:3196-3210(2014).
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}.
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:ETI70664.1}.
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DR   EMBL; ALAN01000011; ETI70664.1; -; Genomic_DNA.
DR   RefSeq; WP_024026486.1; NZ_ALAN01000011.1.
DR   AlphaFoldDB; W1SRJ2; -.
DR   STRING; 220686.AA980_06300; -.
DR   PATRIC; fig|1131730.3.peg.280; -.
DR   eggNOG; COG0150; Bacteria.
DR   OrthoDB; 9802507at2; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000018877; 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:UP000018877}.
FT   DOMAIN          56..160
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          174..336
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   344 AA;  36857 MW;  62B2C42B3E94A382 CRC64;
     MANAYKQAGV NIEAGYEAVE RMKKHVQRTA RTGVLGSLGG FGGMFDLSAL GLKEPVLVSG
     TDGVGTKLMI AFMMDRHDTI GIDAVAMCVN DIVVQGAEPL YFLDYIACGK AVPEKIEAIV
     KGIADGCEQA GCALIGGETA EMPGLYREDE YDLAGFSVGA CEKSALITGE TIAQGDVLIG
     LASSGIHSNG YSLVRKVFNN WSLIEFVDVL GCTLGEELLK PTKIYVKPIL SALKKFKIKG
     MAHITGGGFI ENIPRMLPAG LGADLNEKNW HIPSVFKLIS EVGQIDYREM YNIFNMGVGM
     VIAVDKKDAP ELLEHFHAEG ETAYELGIVT NQAGLNIKGF GGRR
//
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