(data stored in SCRATCH zone)

SWISSPROT: Q3Z4P1_SHISS

ID   Q3Z4P1_SHISS            Unreviewed;       355 AA.
AC   Q3Z4P1;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 100.
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:AAZ87271.1};
GN   OrderedLocusNames=SSON_0496 {ECO:0000313|EMBL:AAZ87271.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87271.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87271.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87271.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ87271.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87271; AAZ87271; SSON_0496.
DR   KEGG; ssn:SSON_0496; -.
DR   HOGENOM; HOG000034026; -.
DR   KO; K01589; -.
DR   OMA; APRTHNS; -.
DR   BioCyc; SSON300269:G1GL2-571-MONOMER; -.
DR   UniPathway; UPA00074; UER00942.
DR   Proteomes; UP000002529; 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; Q3Z4P1.
DR   SWISS-2DPAGE; Q3Z4P1.
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:UP000002529};
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;  39481 MW;  9A85A07FB080595B CRC64;
     MKQVCVLGNG QLGRMLRQAG EPLGIAVWPV GLDAEPAAVP FQQSVITAEI ERWPETALTR
     ELARHPAFVN RDVFPIIADR LTQKQLFDKL HLPTAPWQLL ADRSEWPAVF DRLGELAIVK
     RRTGGYDGRG QWRLRANETE QLPAECYGEC IVEQGINFSG EVSLVGARGF DGSTVFYTLT
     HNLHQDGILR TSVAFPQANA QQQAQAEEML SAIMQELGYV GVMAMECFVT PQGLLINELA
     PRVHNSGHWT QNGASISQFE LHLRAITDLP LPQPVVNNPS VMINLIGSDV NYDWLKLPLV
     HLHWYDKEVR PGRKVGHLNL TDSDTSRLTA TLEALIPLLP PEYASGVIWA QSKFS
//

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