ID A0A172ZD39_9BACL Unreviewed; 394 AA.
AC A0A172ZD39;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=AR543_05860 {ECO:0000313|EMBL:ANF95574.1};
OS Paenibacillus bovis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF95574.1, ECO:0000313|Proteomes:UP000078148};
RN [1] {ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|Proteomes:UP000078148};
RA Wu Z., Gao C., Liu Z., Zheng H.;
RT "Genome of Paenibacillus bovis sp. nov.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANF95574.1, ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|EMBL:ANF95574.1,
RC ECO:0000313|Proteomes:UP000078148};
RX PubMed=26769366; DOI=10.1099/ijsem.0.000900;
RA Gao C., Han J., Liu Z., Xu X., Hang F., Wu Z.;
RT "Paenibacillus bovis sp. nov., isolated from raw yak (Bos grunniens)
RT milk.";
RL Int. J. Syst. Evol. Microbiol. 66:1413-1418(2016).
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; CP013023; ANF95574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A172ZD39; -.
DR STRING; 1616788.AR543_05860; -.
DR KEGG; pbv:AR543_05860; -.
DR UniPathway; UPA00074; UER00942.
DR Proteomes; UP000078148; 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 SMART; SM01209; GARS_A; 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:UP000078148}.
FT DOMAIN 120..308
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 161..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 193..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 278..279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
SQ SEQUENCE 394 AA; 42854 MW; CEE0DC7A5CEC82AF CRC64;
MMEHNHNRPQ AGKVIAPGAT VGILGGGQLG RMMVLQGAPL GYRFITLDPA PDSPCGQVSR
QITAAYDDVE AARRLAEQAD VITYEFENVD AGVAALLAEQ SYVPQGSHLL YTTQHRLREK
RAIEAAGATV APYAEVTSAA ETLAAVQKFG TPCVLKTATG GYDGKGQFVI RTEEQAIQAY
EELSAAGTEL VVEQFIHFQC ELSVIAARST QGEITTFPVA ENIHVDNILH LSIVPARVPE
DVQRRAEQMA ADIAESMNAV GLLAVELFCT ADGQLYVNEL APRPHNSGHY TMEACATSQF
EQHVRAICGL PLGSTALRTP VVMVNILGEH IPDVVERMVS TDAAAEQLNV VPKYHLYGKE
EAKHKRKMGH INVLCHNIED ALAWINQTNI WRNK
//
