(data stored in SCRATCH zone)

SWISSPROT: B7UKJ9_ECO27

ID   B7UKJ9_ECO27            Unreviewed;       355 AA.
AC   B7UKJ9;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
DE            Short=N5-CAIR synthase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
DE            EC=6.3.4.18 {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200};
GN   Name=purK {ECO:0000256|HAMAP-Rule:MF_01928,
GN   ECO:0000256|RuleBase:RU361200, ECO:0000313|EMBL:CAS08003.1};
GN   OrderedLocusNames=E2348C_0455 {ECO:0000313|EMBL:CAS08003.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08003.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08003.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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:0000256|HAMAP-Rule:MF_01928}.
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:0000256|RuleBase:RU361200}.
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:0000256|HAMAP-Rule:MF_01928,
CC         ECO:0000256|RuleBase:RU361200};
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:0000256|HAMAP-Rule:MF_01928, ECO:0000256|RuleBase:RU361200}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01928,
CC       ECO:0000256|RuleBase:RU361200, ECO:0000256|SAAS:SAAS01092012}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000256|HAMAP-
CC       Rule:MF_01928, ECO:0000256|RuleBase:RU361200,
CC       ECO:0000256|SAAS:SAAS01092022}.
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DR   EMBL; FM180568; CAS08003.1; -; Genomic_DNA.
DR   RefSeq; WP_000815561.1; NC_011601.1.
DR   EnsemblBacteria; CAS08003; CAS08003; E2348C_0455.
DR   KEGG; ecg:E2348C_0455; -.
DR   HOGENOM; HOG000034026; -.
DR   KO; K01589; -.
DR   OMA; APRTHNS; -.
DR   BioCyc; ECOL574521:E2348C_RS02385-MONOMER; -.
DR   UniPathway; UPA00074; UER00942.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; B7UKJ9.
DR   SWISS-2DPAGE; B7UKJ9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01928, ECO:0000256|PROSITE-
KW   ProRule:PRU00409, ECO:0000256|RuleBase:RU361200,
KW   ECO:0000256|SAAS:SAAS00098858};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01928,
KW   ECO:0000256|RuleBase:RU361200};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01928,
KW   ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|RuleBase:RU361200,
KW   ECO:0000256|SAAS:SAAS00467005};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01928,
KW   ECO:0000256|RuleBase:RU361200, ECO:0000256|SAAS:SAAS00467012}.
FT   DOMAIN       84    267       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   NP_BIND     125    131       ATP. {ECO:0000256|HAMAP-Rule:MF_01928}.
FT   NP_BIND     153    156       ATP. {ECO:0000256|HAMAP-Rule:MF_01928}.
FT   NP_BIND     237    238       ATP. {ECO:0000256|HAMAP-Rule:MF_01928}.
FT   BINDING      80     80       ATP. {ECO:0000256|HAMAP-Rule:MF_01928}.
FT   BINDING     120    120       ATP. {ECO:0000256|HAMAP-Rule:MF_01928}.
FT   BINDING     161    161       ATP. {ECO:0000256|HAMAP-Rule:MF_01928}.
FT   BINDING     184    184       ATP. {ECO:0000256|HAMAP-Rule:MF_01928}.
SQ   SEQUENCE   355 AA;  39510 MW;  5992BA4646432D7D CRC64;
     MKQVCVLGNG QLGRMLRQAG EPLGIAVWPV GLDAEPAAVP FQQSVITAEI ERWPETALTR
     ELARHPAFVN RDVFPIIADR LTQKQLFDKL HLPTAPWQLL AERSEWPAVF DRLGELAIVK
     RRTGGYDGRG QWRLRAAETE QLPAECYGEC IVEQGINFSG EVSLVGARGF DGSTVFYPLT
     HNLHQDGILR TSVAFPQANA QQQAQAEEML SAIMQELSYV GVMAMECFVT PQGLLINELA
     PRVHNSGHWT QNGASISQFE LHLRAITDLP LPQPVVNNPS VMINLIGSDL NYDWLKLPLV
     HLHWYDKEVR PGRKVGHLNL TDSDTSRLTA TLEALIPLLP PEYASGVMWA QSKFS
//

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