(data stored in ACNUC10821 zone)

SWISSPROT: C8U2K3_ECO10

ID   C8U2K3_ECO10            Unreviewed;       355 AA.
AC   C8U2K3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 65.
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:BAI29361.1};
GN   OrderedLocusNames=ECO103_0494 {ECO:0000313|EMBL:BAI29361.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29361.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29361.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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; AP010958; BAI29361.1; -; Genomic_DNA.
DR   RefSeq; WP_000815553.1; NC_013353.1.
DR   SMR; C8U2K3; -.
DR   EnsemblBacteria; BAI29361; BAI29361; ECO103_0494.
DR   KEGG; eoh:ECO103_0494; -.
DR   HOGENOM; HOG000034026; -.
DR   KO; K01589; -.
DR   OMA; APRTHNS; -.
DR   BioCyc; ECOL585395:ECO103_RS02580-MONOMER; -.
DR   UniPathway; UPA00074; UER00942.
DR   Proteomes; UP000000959; 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; C8U2K3.
DR   SWISS-2DPAGE; C8U2K3.
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:UP000000959};
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;  39482 MW;  9FF951211E44C7C2 CRC64;
     MKQVCVLGNG QLGRMLRQAG EPLGIAVWPV GLDAEPAAVP FQQSVITAEI ERWPETALTR
     ELARHPAFVN RDVFPIIADR LTQKQLFDKL HLPTAPWQLL ADRSEWPAVF ERLGELAIVK
     RRTGGYDGRG QWRLRANETE QLPAECYGEC IVEQGINFSG EVSLVGARGF DGSTVFYPLT
     HNLHQDGILR TSVAFPQANA QQQAQAEEML SAIMQELGYV GVMAMECFVT PQGLLINELA
     PRVHNSGHWT QNGASISQFE LHLRAITDLP LPQPVVNSPS VMINLIGSDV NYDWLKLPLV
     HLHWYDKEVR PGRKVGHLNL TDSDTSRLTA TLEALIPLLP PEYASGVMWA QSKFS
//

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