ID   RHAD_YERPG              Reviewed;         274 AA.
AC   A9QYS3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=YpAngola_A0745;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
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}.
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DR   EMBL; CP000901; ABX85270.1; -; Genomic_DNA.
DR   RefSeq; WP_002209103.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9QYS3; -.
DR   SMR; A9QYS3; -.
DR   GeneID; 57974277; -.
DR   KEGG; ypg:YpAngola_A0745; -.
DR   PATRIC; fig|349746.12.peg.1693; -.
DR   OMA; SHFMSHI; -.
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_1000193739"
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;  30352 MW;  ADBD42F7DDAC6BE0 CRC64;
     MQAILSSWFI QGMIKATSDM WHKGWDERNG GNISLRLLAE EVEPYRRDFY QQPRKVELTQ
     PAPELANSWF LVTGSGKFFR NVELNPAENL VLLQVSNDGM AYHIHWGLTQ GGLPTSELAA
     HFQSHIVRMQ VSGGTNRVIM HCHATNLIAL SYVQKLENAS FTRLLWEGST ECLVVFPDGI
     GIVPWMVPGT DGIGTQTAEQ MREHSLVLWP FHGIFGSGPT LDDAFGLIDT AEKSAEIMVK
     VLSMGGKKQT ISREQLIALA ARFDVTPMAA ALDA