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Database: UniProt
Entry: P9WHL8
LinkDB: P9WHL8
Original site: P9WHL8 
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   16-JAN-2019, entry version 26.
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.,
RA   Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA   Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA   Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA   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-
CC       aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-
CC       carboxyaminoimidazole ribonucleotide (N5-CAIR).
CC       {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-
CC         ribosyl)imidazole + ADP + 2 H(+) + phosphate;
CC         Xref=Rhea:RHEA:19317, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58730,
CC         ChEBI:CHEBI:137981, ChEBI:CHEBI:456216; EC=6.3.4.18;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01928};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-
CC       amino-1-(5-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}.
DR   EMBL; AE000516; AAK47717.1; -; Genomic_DNA.
DR   PIR; E70979; E70979.
DR   RefSeq; WP_003417126.1; NZ_KK341227.1.
DR   ProteinModelPortal; P9WHL8; -.
DR   SMR; P9WHL8; -.
DR   EnsemblBacteria; AAK47717; AAK47717; MT3376.
DR   KEGG; mtc:MT3376; -.
DR   PATRIC; fig|83331.31.peg.3633; -.
DR   KO; K01589; -.
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; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02222; ATP-grasp; 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; Complete proteome; Ligase; Nucleotide-binding;
KW   Purine biosynthesis.
FT   CHAIN         1    429       N5-carboxyaminoimidazole ribonucleotide
FT                                synthase.
FT                                /FTId=PRO_0000428162.
FT   DOMAIN      121    310       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01928}.
FT   NP_BIND     194    197       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     280    281       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     117    117       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     157    157       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     202    202       ATP. {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
//
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