ID   RHAD_LISMO              Reviewed;         273 AA.
AC   Q8Y3I8;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=lmo2847;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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   -!- 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}.
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DR   EMBL; AL591984; CAD01060.1; -; Genomic_DNA.
DR   PIR; AF1430; AF1430.
DR   RefSeq; NP_466369.1; NC_003210.1.
DR   RefSeq; WP_009924506.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y3I8; -.
DR   SMR; Q8Y3I8; -.
DR   STRING; 169963.lmo2847; -.
DR   PaxDb; Q8Y3I8; -.
DR   EnsemblBacteria; CAD01060; CAD01060; CAD01060.
DR   GeneID; 986387; -.
DR   KEGG; lmo:lmo2847; -.
DR   PATRIC; fig|169963.11.peg.2918; -.
DR   eggNOG; COG0235; Bacteria.
DR   HOGENOM; CLU_076831_0_0_9; -.
DR   OMA; SHFMSHI; -.
DR   PhylomeDB; Q8Y3I8; -.
DR   BioCyc; LMON169963:LMO2847-MON; -.
DR   UniPathway; UPA00541; UER00603.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central.
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:0019323; P:pentose catabolic process; IBA:GO_Central.
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; Reference proteome; Rhamnose metabolism;
KW   Zinc.
FT   CHAIN           1..273
FT                   /note="Rhamnulose-1-phosphate aldolase"
FT                   /id="PRO_0000209665"
FT   ACT_SITE        117
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
SQ   SEQUENCE   273 AA;  30430 MW;  C8172956EF6A627B CRC64;
     MTKDIMDAVF IKEMAKTTSN LYRLGWDERN GGNITYLLDE KEVAEYLDVK QIIRTIPMDF
     DGKKLAGKYF LVTGSGKYFK NVEEAPAVNL GVIQVSEDGK AVHLLWGYTD GGLPTSELPA
     HFMSHIARLS VDPENRVVMH CHATHLLAMT FTHELTERAF TRTLWQMCTE CLVVFPEGVG
     IIPWLVPGTN EIGEATSEKM KENRLIVWPH HGIYGAGQSM DETFGLIETA EKAAEVYTIV
     MSQGGIKQAI TDEQLKALGE RFGVEAKAGY LNN