ID   RHAD_SALTY              Reviewed;         275 AA.
AC   Q8ZKS1;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=STM4045;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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   -!- 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; AE006468; AAL22885.1; -; Genomic_DNA.
DR   RefSeq; NP_462926.1; NC_003197.2.
DR   RefSeq; WP_001179685.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZKS1; -.
DR   SMR; Q8ZKS1; -.
DR   STRING; 99287.STM4045; -.
DR   PaxDb; Q8ZKS1; -.
DR   EnsemblBacteria; AAL22885; AAL22885; STM4045.
DR   GeneID; 1255572; -.
DR   KEGG; stm:STM4045; -.
DR   PATRIC; fig|99287.12.peg.4262; -.
DR   HOGENOM; CLU_076831_0_0_6; -.
DR   OMA; SHFMSHI; -.
DR   PhylomeDB; Q8ZKS1; -.
DR   BioCyc; SENT99287:STM4045-MON; -.
DR   UniPathway; UPA00541; UER00603.
DR   Proteomes; UP000001014; 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..275
FT                   /note="Rhamnulose-1-phosphate aldolase"
FT                   /id="PRO_0000209670"
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   275 AA;  30157 MW;  B0EAEE7B0C6AC3E0 CRC64;
     MQNITDSWFV QGMIKATSDA WLKGWDERNG GNLTLRLDEA DIAPFAANFH EKPRYIALSQ
     PMPLLANTPF IVTGSGKFFR NVQLDPAANL GVVKIDSDGA GYHILWGLTH DAVPTSELPA
     HFLSHCERIK ATHGKDRVIM HCHATNLIAL TYVLENNTAL ITRKLWEGST ECLVVFPDGV
     GILPWMVPGT DEIGQATAQE MQKHSLVLWP FHGVFGSGPT LDETFGLIDT AEKSAEVLVK
     IYSMGGMKQT ITREELVALG KRFGVTPLAS AVALY