ID U5L4V3_9BACI Unreviewed; 386 AA.
AC U5L4V3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
DE Short=N5-CAIR synthase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
DE EC=6.3.4.18 {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
GN Name=purK {ECO:0000256|HAMAP-Rule:MF_01928,
GN ECO:0000256|RuleBase:RU361200};
GN ORFNames=N288_01665 {ECO:0000313|EMBL:AGX02305.1};
OS Bacillus infantis NRRL B-14911.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1367477 {ECO:0000313|EMBL:AGX02305.1, ECO:0000313|Proteomes:UP000017805};
RN [1] {ECO:0000313|EMBL:AGX02305.1, ECO:0000313|Proteomes:UP000017805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-14911 {ECO:0000313|EMBL:AGX02305.1,
RC ECO:0000313|Proteomes:UP000017805};
RA Massilamany C., Smith T.P.L., Loy J.D., Barletta R., Reddy J.;
RT "Complete genome sequence of Bacillus infantis NRRL B-14911 that has
RT potential to induce cardiac disease by antigenic mimicry.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole
CC ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole
CC ribonucleotide (N5-CAIR). {ECO:0000256|HAMAP-Rule:MF_01928}.
CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole
CC ribonucleotide (AIR) and HCO(3)- to N5-carboxyaminoimidazole
CC ribonucleotide (N5-CAIR). {ECO:0000256|RuleBase:RU361200}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP +
CC hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole +
CC ADP + 2 H(+) + phosphate; Xref=Rhea:RHEA:19317, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58730, ChEBI:CHEBI:137981, ChEBI:CHEBI:456216;
CC EC=6.3.4.18; Evidence={ECO:0000256|HAMAP-Rule:MF_01928,
CC ECO:0000256|RuleBase:RU361200};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
CC {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01928,
CC ECO:0000256|RuleBase:RU361200}.
CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000256|HAMAP-
CC Rule:MF_01928, ECO:0000256|RuleBase:RU361200}.
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DR EMBL; CP006643; AGX02305.1; -; Genomic_DNA.
DR AlphaFoldDB; U5L4V3; -.
DR STRING; 1367477.N288_01665; -.
DR KEGG; bif:N288_01665; -.
DR PATRIC; fig|1367477.3.peg.275; -.
DR HOGENOM; CLU_011534_0_1_9; -.
DR UniPathway; UPA00074; UER00942.
DR Proteomes; UP000017805; Chromosome.
DR GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:InterPro.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR HAMAP; MF_01928; PurK; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR005875; PurK.
DR InterPro; IPR040686; PurK_C.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR01161; purK; 1.
DR PANTHER; PTHR11609:SF5; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1.
DR PANTHER; PTHR11609; PURINE BIOSYNTHESIS PROTEIN 6/7, PUR6/7; 1.
DR Pfam; PF02222; ATP-grasp; 1.
DR Pfam; PF17769; PurK_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01928};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01928};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01928}; Reference proteome {ECO:0000313|Proteomes:UP000017805}.
FT DOMAIN 114..300
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT BINDING 110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 155..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 185..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 270..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
SQ SEQUENCE 386 AA; 42457 MW; 92139AFD529CB1C8 CRC64;
MNLSKQTILP GQTIGIIGGG QLGRMMALAA KAQGFRIAVL DPAPDSPCGQ VADRQIVGGY
DNLLCIKELA EASDVITYEF ENINAEALDW LTSHAYVPQG SELLRITQDR LTEKEAIERA
GAKVAPYARI EKTADIYDNI EKLDFPAVLK TARGGYDGKG QYVIRSKDDI PEAAELLEKG
ICVLEKWISF QKEISVIIAR NPDGETAVFP VGENIHKDNI LHETIVPAHI SESAARKAED
LAKRIGKALG LVGTLAVEMF LSDGDEIYIN ELAPRPHNSG HYTIEACETS QFEQHIRAVC
NWPLGSTRLL NPAVMVNILG EHQSDVIRAI PGLKDWKIHL YGKDEPKHKR KMGHATLLRP
TAAESLAEID RSGIWSKAKE GMEVLR
//
