ID   RHAD_ECODH              Reviewed;         274 AA.
AC   B1XB69;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
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};
GN   OrderedLocusNames=ECDH10B_4092;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/jb.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into the
RT   biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000948; ACB04915.1; -; Genomic_DNA.
DR   RefSeq; WP_001179745.1; NC_010473.1.
DR   AlphaFoldDB; B1XB69; -.
DR   SMR; B1XB69; -.
DR   KEGG; ecd:ECDH10B_4092; -.
DR   HOGENOM; CLU_076831_0_0_6; -.
DR   OMA; SHFMSHI; -.
DR   BioCyc; ECOL316385:ECDH10B_RS20830-MON; -.
DR   UniPathway; UPA00541; UER00603.
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_1000193721"
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;  30145 MW;  F9FF0BE156F4E63D CRC64;
     MQNITQSWFV QGMIKATTDA WLKGWDERNG GNLTLRLDDA DIAPYHDNFH QQPRYIPLSQ
     PMPLLANTPF IVTGSGKFFR NVQLDPAANL GIVKVDSDGA GYHILWGLTN EAVPTSELPA
     HFLSHCERIK ATNGKDRVIM HCHATNLIAL TYVLENDTAV FTRQLWEGST ECLVVFPDGV
     GILPWMVPGT DEIGQATAQE MQKHSLVLWP FHGVFGSGPT LDETFGLIDT AEKSAQVLVK
     VYSMGGMKQT ISREELIALG KRFGVTPLAS ALAL