ID PUR5_BRUA2 Reviewed; 359 AA.
AC Q2YN59;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000255|HAMAP-Rule:MF_00741};
DE EC=6.3.3.1 {ECO:0000255|HAMAP-Rule:MF_00741};
DE AltName: Full=AIR synthase {ECO:0000255|HAMAP-Rule:MF_00741};
DE AltName: Full=AIRS {ECO:0000255|HAMAP-Rule:MF_00741};
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000255|HAMAP-Rule:MF_00741};
GN Name=purM {ECO:0000255|HAMAP-Rule:MF_00741}; OrderedLocusNames=BAB1_0731;
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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:0000255|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. {ECO:0000255|HAMAP-
CC Rule:MF_00741}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00741}.
CC -!- SIMILARITY: Belongs to the AIR synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00741}.
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DR EMBL; AM040264; CAJ10687.1; -; Genomic_DNA.
DR RefSeq; WP_002963853.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YN59; -.
DR SMR; Q2YN59; -.
DR STRING; 359391.BAB1_0731; -.
DR GeneID; 58776159; -.
DR KEGG; bmf:BAB1_0731; -.
DR PATRIC; fig|359391.11.peg.3044; -.
DR HOGENOM; CLU_047116_0_0_5; -.
DR PhylomeDB; Q2YN59; -.
DR UniPathway; UPA00074; UER00129.
DR PRO; PR:Q2YN59; -.
DR Proteomes; UP000002719; Chromosome I.
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; Cytoplasm; Ligase; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..359
FT /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT /id="PRO_0000258337"
SQ SEQUENCE 359 AA; 37447 MW; 594BAB33E3F569F7 CRC64;
MTMENKPAGQ NGLTYAQAGV DIDAGNLMVE KIKPLVRSTR RPGADGEIGG FGGLFDLKAA
GFKDPVLVAA NDGVGTKLKI AIDADIHDTV GIDLVAMCVN DLVVQGAEPL FFLDYYATGK
LSPDQGVAIV SGIAEGCRQA GCALIGGETA EMPGMYRDGD YDLAGFAVGA AERDRLLPRG
DIAEGDIILG LASSGVHSNG FSLVRRIVEL SGLGWKSQAP FQPGATLGEA LLTPTRIYVK
PLLAAIRACD GIKALAHITG GGFPDNIPRV LPKGLAAEID LPAIAVPPVF SWLAKTGNVE
PNEMLRTFNC GIGMIAVVNP AKVDEVIAAL AAEGEKVVTL GRMTRREKDG VIYKGQLAL
//
