ID A0A2E7NX38_9BURK Unreviewed; 401 AA.
AC A0A2E7NX38;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=CME87_01000 {ECO:0000313|EMBL:MBO14041.1};
OS Herbaspirillum sp.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1890675 {ECO:0000313|EMBL:MBO14041.1, ECO:0000313|Proteomes:UP000226028};
RN [1] {ECO:0000313|Proteomes:UP000226028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Graham E.D., Heidelberg J.F.;
RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT Global Oceans.";
RL Submitted (SEP-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MBO14041.1}.
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DR EMBL; PBPP01000013; MBO14041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2E7NX38; -.
DR UniPathway; UPA00074; UER00942.
DR Proteomes; UP000226028; Unassembled WGS sequence.
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}.
FT DOMAIN 126..312
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 166..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 196..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
FT BINDING 282..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01928"
SQ SEQUENCE 401 AA; 42142 MW; FEBD9DB3A2A1E933 CRC64;
MTQQSASTLR PAVPSTTPAT WLGVMGGGQL GRMFAHAAQS MGFKVAVLEA DADCPAGQVA
DRLINAAYDD GAALAELGAL CAAITTEFEN VSAKSLATLA AQTFVAPAAS GVSIAQDRTA
EKAFFTECGS QSGVLPAPHL VINSAADIDG LDAKLLPGIL KTARMGYDGK GQVRVRTVDE
VRAAFAAMKG VTCVLEKMLP LAYEVSVLVA RGHDGQAVVY PIAENVHRDG ILFTTTVPGP
NIKADAAARA QQAALQIIGA MHYVGVLCIE FFVLDDGALV VNEMAPRPHN SGHYTIDACV
TSQFEQQARA MARLPLGDTR QHSPSVMLNI LGDVWYEGDT DAQREPAWDQ VLALPGAHLH
LYGKAEARRG RKMGHVTFTG ATLADAQRQL AAACAILGIT L
//
