PURK_PSEAE
ID PURK_PSEAE Reviewed; 360 AA.
AC P72158;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 133.
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}; OrderedLocusNames=PA5425;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAK;
RX PubMed=8816818; DOI=10.1073/pnas.93.19.10434;
RA Wang J., Mushegian A., Lory S., Jin S.;
RT "Large-scale isolation of candidate virulence genes of Pseudomonas
RT aeruginosa by in vivo selection.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10434-10439(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; U58364; AAB17258.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08810.1; -; Genomic_DNA.
DR PIR; G82967; G82967.
DR RefSeq; NP_254112.1; NC_002516.2.
DR RefSeq; WP_003096798.1; NZ_QZGE01000012.1.
DR AlphaFoldDB; P72158; -.
DR SMR; P72158; -.
DR STRING; 287.DR97_2802; -.
DR PaxDb; P72158; -.
DR PRIDE; P72158; -.
DR EnsemblBacteria; AAG08810; AAG08810; PA5425.
DR GeneID; 878440; -.
DR KEGG; pae:PA5425; -.
DR PATRIC; fig|208964.12.peg.5685; -.
DR PseudoCAP; PA5425; -.
DR HOGENOM; CLU_011534_0_1_6; -.
DR InParanoid; P72158; -.
DR OMA; ITFDHEH; -.
DR PhylomeDB; P72158; -.
DR BioCyc; PAER208964:G1FZ6-5552-MON; -.
DR UniPathway; UPA00074; UER00942.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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;
KW Reference proteome.
FT CHAIN 1..360
FT /note="N5-carboxyaminoimidazole ribonucleotide synthase"
FT /id="PRO_0000075002"
FT DOMAIN 102..285
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 143..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 173..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 255..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT CONFLICT 124
FT /note="L -> V (in Ref. 1; AAB17258)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="L -> V (in Ref. 1; AAB17258)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="F -> L (in Ref. 1; AAB17258)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="G -> A (in Ref. 1; AAB17258)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="E -> D (in Ref. 1; AAB17258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 38496 MW; 88FBBEA510DE2B54 CRC64;
MKIGVIGGGQ LGRMLALAGT PLGMNFAFLD PAPDACAASL GEHIRADYGD QEHLRQLADE
VDLVTFEFES VPAETVAFLS QFVPVYPNAE SLRIARDRWF EKSMFKDLGI PTPDFADVQS
QADLDAAAAA IGLPAVLKTR TLGYDGKGQK VLRQPADVQG AFAELGSVPC ILEGFVPFTG
EVSLVAVRAR DGETRFYPLV HNTHDSGILK LSVASSGHPL QALAEDYVGR VLARLDYVGV
LAFEFFEVDG GLKANEIAPR VHNSGHWTIE GAECSQFENH LRAVAGLPLG STAKVGESAM
LNFIGAVPPV AQVVAVADCH LHHYGKAFKN GRKVGHATLR CADRATLQAR IAEVEALIEA
