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Database: UniProt
Entry: A0A0A1DRU0_NOCSI
LinkDB: A0A0A1DRU0_NOCSI
Original site: A0A0A1DRU0_NOCSI 
ID   A0A0A1DRU0_NOCSI        Unreviewed;       353 AA.
AC   A0A0A1DRU0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 2.
DT   27-MAR-2024, entry version 41.
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=KR76_23295 {ECO:0000313|EMBL:AIY20136.2};
OS   Nocardioides simplex (Arthrobacter simplex).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Pimelobacter.
OX   NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY20136.2, ECO:0000313|Proteomes:UP000030300};
RN   [1] {ECO:0000313|EMBL:AIY20136.2, ECO:0000313|Proteomes:UP000030300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY20136.2,
RC   ECO:0000313|Proteomes:UP000030300};
RX   PubMed=25573942;
RA   Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA   Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT   "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT   Ac-2033D.";
RL   Genome Announc. 3:0-0(2015).
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}.
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DR   EMBL; CP009896; AIY20136.2; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1DRU0; -.
DR   STRING; 2045.KR76_23295; -.
DR   KEGG; psim:KR76_23295; -.
DR   eggNOG; COG0150; Bacteria.
DR   HOGENOM; CLU_047116_0_0_11; -.
DR   UniPathway; UPA00074; UER00129.
DR   Proteomes; UP000030300; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030300}.
FT   DOMAIN          58..163
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          175..344
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
SQ   SEQUENCE   353 AA;  37051 MW;  784E966E7C3FC8DA CRC64;
     MADNAYARAG VDIEAADRAV DLMKEWVEKA RRPEMRGGLG GFAGLFDASA LLSYRRPLLA
     TSTDGVGTKV AVAQMVDKHD TIGFDLVGMV VDDLVVCGAE PLFMTDYIAT GKVVPERIAA
     IVKGIAEACV EAGCALVGGE TAEHPGLLAP DEYDVAGATT GVVEADALLG ASRVREGDVV
     IAMAASGLHS NGYSLARHVF FTQAGWSVER HVDELGRTLG EELLEPTRLY TKPCLTIARE
     TETHAMAHVT GGGLANNLAR VMPPELKATL DRATWTPGPV FDLVRRLGDV AQPDLEATLN
     CGVGMVALVA PDAVDGALAR LAESGIDSWV AGDVTVDPDQ KGTVELVGQH PGW
//
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