PURK_AQUAE
ID PURK_AQUAE Reviewed; 365 AA.
AC O66608;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
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=aq_245;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC06567.1; -; Genomic_DNA.
DR PIR; D70322; D70322.
DR RefSeq; NP_213168.1; NC_000918.1.
DR RefSeq; WP_010880106.1; NC_000918.1.
DR PDB; 2Z04; X-ray; 2.35 A; A/B=1-365.
DR PDBsum; 2Z04; -.
DR AlphaFoldDB; O66608; -.
DR SMR; O66608; -.
DR STRING; 224324.aq_245; -.
DR EnsemblBacteria; AAC06567; AAC06567; aq_245.
DR KEGG; aae:aq_245; -.
DR PATRIC; fig|224324.8.peg.200; -.
DR eggNOG; COG0026; Bacteria.
DR HOGENOM; CLU_011534_0_0_0; -.
DR InParanoid; O66608; -.
DR OMA; ITFDHEH; -.
DR OrthoDB; 1165275at2; -.
DR UniPathway; UPA00074; UER00942.
DR EvolutionaryTrace; O66608; -.
DR Proteomes; UP000000798; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..365
FT /note="N5-carboxyaminoimidazole ribonucleotide synthase"
FT /id="PRO_0000074993"
FT DOMAIN 97..279
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 137..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 168..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 249..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:2Z04"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:2Z04"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 203..212
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 215..227
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:2Z04"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:2Z04"
FT HELIX 341..353
FT /evidence="ECO:0007829|PDB:2Z04"
SQ SEQUENCE 365 AA; 41988 MW; C8E859448888AA42 CRC64;
MLTVGILGGG QLGWMTILEG RKLGFKFHVL EDKENAPACR VADRCFRTGQ ISEFVDSCDI
ITYEFEHIKD EVLEKCESKL IPNPQALYVK KSRIREKLFL KKHGFPVPEF LVIKRDEIID
ALKSFKLPVV IKAEKLGYDG KGQYRIKKLE DANQVVKNHD KEESFIIEEF VKFEAEISCI
GVRDREGKTY FYPQPFNKHE EGILIYNYVP YAKLKEAEEI TKRLMELLDI VGVFTVEFFL
LKDGRVLINE FAPRVHNTGH WTLDGAYTSQ FENLLRAITE MPLGSTELKL PSGMVNILGK
SYEEIPLKEI LSVEGAKLYW YGKEKKPRRK VGHVNVVGRS KEEVVEKVER VFTLLKGSRE
KLPAP
