ID   RHAD_SHISS              Reviewed;         274 AA.
AC   Q3YV74;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Rhamnulose-1-phosphate aldolase;
DE            EC=4.1.2.19;
GN   Name=rhaD; OrderedLocusNames=SSON_4072;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 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; CP000038; AAZ90588.1; -; Genomic_DNA.
DR   RefSeq; YP_312823.1; -.
DR   SMR; Q3YV74; 1-274.
DR   GeneID; 3669534; -.
DR   GenomeReviews; CP000038_GR; SSON_4072.
DR   KEGG; ssn:SSON_4072; -.
DR   HOGENOM; Q3YV74; -.
DR   OMA; Q3YV74; MSHIARL.
DR   BioCyc; SSON300269:SSO_4072-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_1000017345.
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;  30006 MW;  F41C09D12BD3C24C CRC64;
     MQNITQSWFV QGMIKATTDA WLKGWDERNG GNLTLRLDDA DIAPYHGNFH AQPRYIPLSQ
     PMPLLANTPF IVTGSGKFFR NVQLDPAANL GVVKVDSDGA GYHILWGLTN EAVPTSELPA
     HFLSHCERIK ATNGKDRVIM HCHATNLIAL TYVLENDTAV FTRQLWEGST ECLVVFPDGV
     GILPWMVPGT DEIGQATAQE MQKHSLVLWP FHGVFGSGST LDETFGLIDT AEKSAQVLVK
     VYSMGGMKQT ISREELIALG KRFGVTPLAS ALAL
//