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Database: UniProt
Entry: G4R9X9_PELHB
LinkDB: G4R9X9_PELHB
Original site: G4R9X9_PELHB 
ID   G4R9X9_PELHB            Unreviewed;       364 AA.
AC   G4R9X9;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
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   OrderedLocusNames=KKY_2498 {ECO:0000313|EMBL:AEQ52506.1};
OS   Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 /
OS   B2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Devosiaceae; Pelagibacterium.
OX   NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ52506.1, ECO:0000313|Proteomes:UP000008850};
RN   [1] {ECO:0000313|EMBL:AEQ52506.1, ECO:0000313|Proteomes:UP000008850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2
RC   {ECO:0000313|Proteomes:UP000008850};
RX   PubMed=22156395; DOI=10.1128/JB.06343-11;
RA   Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., Zhu X.F.,
RA   Liu Y.F., Li P.F., Ni P.X., Wu M.;
RT   "Complete genome sequence of Pelagibacterium halotolerans B2T.";
RL   J. Bacteriol. 194:197-198(2012).
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; CP003075; AEQ52506.1; -; Genomic_DNA.
DR   RefSeq; WP_014131655.1; NC_016078.1.
DR   AlphaFoldDB; G4R9X9; -.
DR   STRING; 1082931.KKY_2498; -.
DR   KEGG; phl:KKY_2498; -.
DR   PATRIC; fig|1082931.4.peg.2467; -.
DR   eggNOG; COG0026; Bacteria.
DR   HOGENOM; CLU_011534_0_1_5; -.
DR   OMA; ITFDHEH; -.
DR   UniPathway; UPA00074; UER00942.
DR   Proteomes; UP000008850; 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|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
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:UP000008850}.
FT   DOMAIN          113..303
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT   BINDING         149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT   BINDING         154..160
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         273..274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
SQ   SEQUENCE   364 AA;  38720 MW;  6AC9DD5297F4E850 CRC64;
     MTENHPLQPG GRIGILGGGQ LGRMLSLAAS QLGMKTHIFC PDPESPAFEV TPSKTIAGYD
     DVAALRAFAG DVDVVTYEFE NVPLATAKVI ADNVTLRPGA KALEVSQDRL AEKAFLSHVG
     IAVAPYRAVG SLQDLQAAIS DIGLPAVLKT TRLGYDGKGQ RMIGKPDDIE GAFTELAPGA
     PLVLEAYIPF EKEISVIVVR GTDGSVVTYD PAENVHRNHI LKTSTLPATV SDGLAAKARA
     IAGAIAKALD YVGTMGVEFF VVSDGDDPQV LVNEIAPRVH NSGHWTQAVC VTDQFENHIR
     AICDWPLGDT TRLADVVMEN LIGEEIFATA SRSISGIQPH VYGKAEARTG RKMGHLNIVK
     LPRA
//
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