ID   RHAD_ECOL6              Reviewed;         274 AA.
AC   Q8FBE1;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Rhamnulose-1-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00770};
DE            EC=4.1.2.19 {ECO:0000255|HAMAP-Rule:MF_00770};
GN   Name=rhaD {ECO:0000255|HAMAP-Rule:MF_00770}; OrderedLocusNames=c4851;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate
CC       to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.
CC       {ECO:0000255|HAMAP-Rule:MF_00770}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-rhamnulose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone
CC         phosphate; Xref=Rhea:RHEA:19689, ChEBI:CHEBI:18041,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:58313; EC=4.1.2.19;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00770};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00770};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00770};
CC   -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone
CC       phosphate from L-rhamnose: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00770}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00770}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00770}.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. RhaD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00770}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN83279.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN83279.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001179742.1; NC_004431.1.
DR   AlphaFoldDB; Q8FBE1; -.
DR   SMR; Q8FBE1; -.
DR   STRING; 199310.c4851; -.
DR   EnsemblBacteria; AAN83279; AAN83279; c4851.
DR   KEGG; ecc:c4851; -.
DR   eggNOG; COG0235; Bacteria.
DR   HOGENOM; CLU_076831_0_0_6; -.
DR   OMA; SHFMSHI; -.
DR   UniPathway; UPA00541; UER00603.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008994; F:rhamnulose-1-phosphate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019301; P:rhamnose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.225.10; -; 1.
DR   HAMAP; MF_00770; RhaD; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   InterPro; IPR013447; Rhamnulose-1-P_Aldolase.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53639; SSF53639; 1.
DR   TIGRFAMs; TIGR02624; rhamnu_1P_ald; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Metal-binding; Rhamnose metabolism; Zinc.
FT   CHAIN           1..274
FT                   /note="Rhamnulose-1-phosphate aldolase"
FT                   /id="PRO_0000209658"
FT   ACT_SITE        117
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
SQ   SEQUENCE   274 AA;  30192 MW;  4DFF0BF512ABB842 CRC64;
     MQNITQSWFV QGMIKATTDA WLKGWDERNG GNLTLRLDDA DIAPYHDNFH QQPRYIPLSQ
     PMPLLANTPF IVTGSGKFFR NVQLDPAANL GIVKVDSDGA GYHILWGLTN EAVPTSELPA
     HFLSHCERIK ATNGKDRVIM HCHATNLIAL TYVLENDTAV FTRQLWEGST ECLVVFPDGV
     GILPWMVPGT DEIGQATAQE MQKHSLMLWP FHGVFGSGPT LDETFGLIDT AEKSAQILVK
     VYSMGGMKQT ISREELIALG QRFGVTPLAS ALAL