PURK_SACS2
ID PURK_SACS2 Reviewed; 365 AA.
AC O06457;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=SSO1065;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=9311113; DOI=10.1111/j.1574-6968.1997.tb12640.x;
RA Soerensen I.S., Dandanell G.;
RT "Identification and sequence analysis of Sulfolobus solfataricus purE and
RT purK genes.";
RL FEMS Microbiol. Lett. 154:173-180(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; Y13143; CAA73603.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41328.1; -; Genomic_DNA.
DR PIR; A90259; A90259.
DR RefSeq; WP_009989884.1; NC_002754.1.
DR AlphaFoldDB; O06457; -.
DR SMR; O06457; -.
DR STRING; 273057.SSO1065; -.
DR PRIDE; O06457; -.
DR EnsemblBacteria; AAK41328; AAK41328; SSO1065.
DR GeneID; 44129999; -.
DR KEGG; sso:SSO1065; -.
DR PATRIC; fig|273057.12.peg.1062; -.
DR eggNOG; arCOG01597; Archaea.
DR HOGENOM; CLU_011534_0_0_2; -.
DR InParanoid; O06457; -.
DR OMA; ITFDHEH; -.
DR PhylomeDB; O06457; -.
DR UniPathway; UPA00074; UER00942.
DR Proteomes; UP000001974; Chromosome.
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..365
FT /note="N5-carboxyaminoimidazole ribonucleotide synthase"
FT /id="PRO_0000075020"
FT DOMAIN 106..286
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 148..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 177..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 256..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
SQ SEQUENCE 365 AA; 42360 MW; A9EE75D029EE199C CRC64;
MFSVLDWKPK IGILGGGQLG WMIVLEGRKY PFTFYVLEND KNAPACRIAD RCFSPQDYKE
FVDSSDVITF EFEHVYEKAL EYAEYSGKLL PRLNSVELKR ERYKEKLFYR QHNLPTPRFY
VAEDGEEALK ILREEFNNVG VIKESKGGYD GKGQYFIFND VEKYQFLREK KEKMVVEEYV
KFDFEASIII ARDKRGVFIS YPPTYNYNEK GILVYNYGPY NNQNIVEIAR RLSEELDYVG
IMGVEVFVVN GKVLINEFAP RVHNTGHYTL DGALISQFEQ HLRAIIGMEL GPSTILSPSG
MVNILGTDKI PVEVLKYGKV YWYSKSEVRK RRKMGHVNVV GNNLEEVKQK IDKIMQLIYT
NGLDL
