PURK_SYNE7
ID PURK_SYNE7 Reviewed; 395 AA.
AC Q54975; Q31NB1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000255|HAMAP-Rule:MF_01928};
DE Short=N5-CAIR synthase {ECO:0000255|HAMAP-Rule:MF_01928};
DE EC=6.3.4.18 {ECO:0000255|HAMAP-Rule:MF_01928};
DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_01928};
GN Name=purK {ECO:0000255|HAMAP-Rule:MF_01928};
GN OrderedLocusNames=Synpcc7942_1428;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lieman-Hurwitz J., Bonfil D., Ronen-Tarazi M., Kaplan A.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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:0000255|HAMAP-Rule:MF_01928}.
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:0000255|HAMAP-Rule:MF_01928};
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:0000255|HAMAP-Rule:MF_01928}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01928}.
CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC Rule:MF_01928}.
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DR EMBL; U62615; AAB05791.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57458.1; -; Genomic_DNA.
DR RefSeq; WP_011242442.1; NC_007604.1.
DR AlphaFoldDB; Q54975; -.
DR SMR; Q54975; -.
DR STRING; 1140.Synpcc7942_1428; -.
DR PRIDE; Q54975; -.
DR EnsemblBacteria; ABB57458; ABB57458; Synpcc7942_1428.
DR KEGG; syf:Synpcc7942_1428; -.
DR eggNOG; COG0026; Bacteria.
DR HOGENOM; CLU_011534_0_2_3; -.
DR OMA; ITFDHEH; -.
DR OrthoDB; 1165275at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1428-MON; -.
DR UniPathway; UPA00074; UER00942.
DR GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 3.30.1490.20; -; 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 Pfam; PF02222; ATP-grasp; 1.
DR Pfam; PF17769; PurK_C; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01161; purK; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..395
FT /note="N5-carboxyaminoimidazole ribonucleotide synthase"
FT /id="PRO_0000075013"
FT DOMAIN 113..298
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 184..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 268..269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT CONFLICT 59
FT /note="A -> R (in Ref. 1; AAB05791)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 42459 MW; 305196BD699FF228 CRC64;
MNAIAVSPVQ HVGVIGGGQL AWMLAPAAQQ LGMSLHVQTP NDHDPAVAIA DQTVLAAVAD
AAATAKLAQA CDVITFENEF VDLPALTELE ETGVRFRPRP AAIASLLDKL DQRQLLTRLG
LPTPRFLAIA AATATESELT ALGFPVVLKQ RRHGYDGKGT QVLRSLAELQ QALQSYGDTP
LLLEEFIPFE QELAVMVARS QSGAIATFPV VQTHQQNQVC RWVVAPAAIP GALQKAVAAI
ARTLVETVDY VGVAGIELFQ QGDRLWVNEI APRTHNSGHY SLDACQTSQF EQQLRAIADL
PLGSTALQWP GALMVNLLGF EDHQSGYAEL RQQLAALPGA CLYWYGKTES KPGRKLGHIT
LPLSGASSTE RAQQAQTMLA QVEAIWPNPD TAHQP
