PURK_MYCTO
ID PURK_MYCTO Reviewed; 429 AA.
AC P9WHL8; L0TEV0; P65898; P96881;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
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=MT3376;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK47717.1; -; Genomic_DNA.
DR PIR; E70979; E70979.
DR RefSeq; WP_003417126.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WHL8; -.
DR SMR; P9WHL8; -.
DR EnsemblBacteria; AAK47717; AAK47717; MT3376.
DR KEGG; mtc:MT3376; -.
DR PATRIC; fig|83331.31.peg.3633; -.
DR HOGENOM; CLU_011534_0_2_11; -.
DR UniPathway; UPA00074; UER00942.
DR Proteomes; UP000001020; 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.
FT CHAIN 1..429
FT /note="N5-carboxyaminoimidazole ribonucleotide synthase"
FT /id="PRO_0000428162"
FT DOMAIN 121..310
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT REGION 406..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 194..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
FT BINDING 280..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01928"
SQ SEQUENCE 429 AA; 45695 MW; 1A80B4CCAB8CB13E CRC64;
MMAVASSRTP AVTSFIAPLV AMVGGGQLAR MTHQAAIALG QNLRVLVTSA DDPAAQVTPN
VVIGSHTDLA ALRRVAAGAD VLTFDHEHVP NELLEKLVAD GVNVAPSPQA LVHAQDKLVM
RQRLAAAGVA VPRYAGIKDP DEIDVFAARV DAPIVVKAVR GGYDGRGVRM ARDVADARDF
ARECLADGVA VLVEERVDLR RELSALVARS PFGQGAAWPV VQTVQRDGTC VLVIAPAPAL
PDDLATAAQR LALQLADELG VVGVLAVELF ETTDGALLVN ELAMRPHNSG HWTIDGARTS
QFEQHLRAVL DYPLGDSDAV VPVTVMANVL GAAQPPAMSV DERLHHLFAR MPDARVHLYG
KAERPGRKVG HINFLGSDVA QLCERAELAA HWLSHGRWTD GWDPHRASDD AVGVPPACGG
RSDEEERRL
