RHAD_YERPB
ID RHAD_YERPB Reviewed; 274 AA.
AC B2K1W0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=YPTS_0406;
OS Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1/+;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001048; ACC87395.1; -; Genomic_DNA.
DR RefSeq; WP_012413440.1; NZ_CP009780.1.
DR AlphaFoldDB; B2K1W0; -.
DR SMR; B2K1W0; -.
DR KEGG; ypb:YPTS_0406; -.
DR PATRIC; fig|502801.10.peg.4084; -.
DR OMA; SHFMSHI; -.
DR BioCyc; YPSE502801:YPTS_RS02130-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_1000193740"
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; 30361 MW; C297ED8D2A03174F CRC64;
MQAILSSWFI QGMIKATSDM WHKGWDERNG GNISLRLLAE EVEPYRRDFY QHPRKVELTQ
PAPELANSWF LVTGSGKFFR NVELNPAENL VLLQVSNDGM AYHIHWGLTQ GGLPTSELAA
HFQSHIVRMQ VSGGTNRVIM HCHATNLIAL SYVQKLENAS FTRLLWEGST ECLVVFPDGI
GIVPWMVPGT DGIGTQTAEQ MREHSLVLWP FHGIFGSGPT LDDAFGLIDT AEKSAEIMVK
VLSMGGKKQT ISREQLIALA ARFDVTPMAA ALDA