PUR5_RHORT
ID PUR5_RHORT Reviewed; 370 AA.
AC Q2RSC8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 90.
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=Rru_A2167;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC22967.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000230; ABC22967.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_014626325.1; NC_007643.1.
DR RefSeq; YP_427254.1; NC_007643.1.
DR AlphaFoldDB; Q2RSC8; -.
DR SMR; Q2RSC8; -.
DR STRING; 269796.Rru_A2167; -.
DR EnsemblBacteria; ABC22967; ABC22967; Rru_A2167.
DR KEGG; rru:Rru_A2167; -.
DR PATRIC; fig|269796.9.peg.2261; -.
DR eggNOG; COG0150; Bacteria.
DR HOGENOM; CLU_047116_0_0_5; -.
DR OrthoDB; 923547at2; -.
DR PhylomeDB; Q2RSC8; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000001929; 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; 3.30.1330.10; -; 1.
DR Gene3D; 3.90.650.10; -; 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 PANTHER; PTHR10520; PTHR10520; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00878; purM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..370
FT /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT /id="PRO_0000258397"
SQ SEQUENCE 370 AA; 38262 MW; 6ED6331649891FD7 CRC64;
MKNEVAISTS HLDAGATGTG LTYKDAGVDI DSGNALVQAI KPLAASTKRP GADASLGGFG
AIFDLAAAGY SDPLLITATD GVGTKLKIAL DSGIHDSVGI DLVAMCVNDL VVQGGEPLLF
LDYFATSRLQ VPVASAVVKG IAEGCLQAGC ALVGGETAEM PGMYGNNDYD LAGFAVGAVE
RSQLLTDDRI GLGDVLLGLA SSGVHSNGFS LVRRIVERSG LAWDAPAPFA PETTLARALL
TPTRIYVKSC LALHRAGLVH GFAHITGGGF WENIPRVLPQ GACAHLDGLS WPFPPVFRWL
MDQGGVSAHE MARTFNCGIG MVVAVPADKA EAAIALLGEH GETVHRLGTI AARGEGEAVI
IDHLDEAFAR