ID   RHAD_ECOL5              Reviewed;         274 AA.
AC   Q0TAG1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Rhamnulose-1-phosphate aldolase;
DE            EC=4.1.2.19;
GN   Name=rhaD; OrderedLocusNames=ECP_4112;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- FUNCTION: Catalyzes the reversible cleavage of L-rhamnulose-1-
CC       phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-rhamnulose 1-phosphate = glycerone phosphate
CC       + (S)-lactaldehyde.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation;
CC       glycerone phosphate from L-rhamnose: step 3/3.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the aldolase class II family. RhaD
CC       subfamily.
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DR   EMBL; CP000247; ABG72068.1; -; Genomic_DNA.
DR   RefSeq; YP_671969.1; -.
DR   SMR; Q0TAG1; 1-274.
DR   GeneID; 4189732; -.
DR   GenomeReviews; CP000247_GR; ECP_4112.
DR   KEGG; ecp:ECP_4112; -.
DR   HOGENOM; Q0TAG1; -.
DR   OMA; Q0TAG1; MSHIARL.
DR   BioCyc; ECOL362663:ECP_4112-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008994; F:rhamnulose-1-phosphate aldolase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019299; P:rhamnose metabolic process; IEA:HAMAP.
DR   HAMAP; MF_00770; -; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR013447; RhaD.
DR   Gene3D; G3DSA:3.40.225.10; Aldolase_II/adducin_N; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   TIGRFAMs; TIGR02624; rhamnu_1P_ald; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Lyase; Metal-binding;
KW   Rhamnose metabolism; Zinc.
FT   CHAIN         1    274       Rhamnulose-1-phosphate aldolase.
FT                                /FTId=PRO_1000017338.
FT   ACT_SITE    117    117       By similarity.
FT   METAL       141    141       Zinc (By similarity).
FT   METAL       143    143       Zinc (By similarity).
FT   METAL       212    212       Zinc (By similarity).
SQ   SEQUENCE   274 AA;  30159 MW;  3AFF0BE156FBAC06 CRC64;
     MQNITQSWFV QGMIKATTDA WLKGWDERNG GNLTLRLDDA DIAPYHDNFH QQPRYIPLSQ
     PMPLLANTPF IVTGSGKFFR NVQLDPAANL GIVKVDSDGA GYHILWGLTN EAVPTSELPA
     HFLSHCERIK ATNGKDRVIM HCHATNLIAL TYVLENDTAV FTRQLWEGST ECLVVFPDGV
     GILPWMVPGT DEIGQATAQE MQKHSLVLWP FHGVFGSGPT LDETFGLIDT AEKSAQILVK
     VYSMGGMKQT ISREELIALG QRFGVTPLAS ALAL
//