ID RHAD_ECOLI Reviewed; 274 AA. AC P32169; Q2M8J9; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 02-SEP-2026, entry version 170. DE RecName: Full=Rhamnulose-1-phosphate aldolase; DE EC=4.1.2.19 {ECO:0000269|PubMed:12962479}; GN Name=rhaD; Synonyms=rhuA; OrderedLocusNames=b3902, JW3873; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=8396120; DOI=10.1128/jb.175.17.5585-5594.1993; RA Moralejo P., Egan S.M., Hidalgo E.F., Aguilar J.; RT "Sequencing and characterization of a gene cluster encoding the enzymes for RT L-rhamnose metabolism in Escherichia coli."; RL J. Bacteriol. 175:5585-5594(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=8346018; DOI=10.1093/nar/21.15.3391; RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.; RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region RT from 87.2 to 89.2 minutes."; RL Nucleic Acids Res. 21:3391-3398(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP INDUCTION. RC STRAIN=ECL116; RX PubMed=8230210; DOI=10.1006/jmbi.1993.1565; RA Egan S.M., Schleif R.F.; RT "A regulatory cascade in the induction of rhaBAD."; RL J. Mol. Biol. 234:87-98(1993). RN [6] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [7] RP INDUCTION. RX PubMed=10852886; DOI=10.1128/jb.182.12.3529-3535.2000; RA Holcroft C.C., Egan S.M.; RT "Roles of cyclic AMP receptor protein and the carboxyl-terminal domain of RT the alpha subunit in transcription activation of the Escherichia coli RT rhaBAD operon."; RL J. Bacteriol. 182:3529-3535(2000). RN [8] RP FUNCTION. RX PubMed=25848029; DOI=10.1073/pnas.1423570112; RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L., RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D., RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D., RA Allen K.N., Farelli J.D.; RT "Panoramic view of a superfamily of phosphatases through substrate RT profiling."; RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR, RP SUBUNIT, AND ACTIVE SITE. RX PubMed=11976494; DOI=10.1107/s0907444902004614; RA Kroemer M., Schulz G.E.; RT "The structure of L-rhamnulose-1-phosphate aldolase (class II) solved by RT low-resolution SIR phasing and 20-fold NCS averaging."; RL Acta Crystallogr. D 58:824-832(2002). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION, RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, RP AND MUTAGENESIS OF ARG-28; ASN-29; GLU-117; GLU-171 AND GLU-192. RX PubMed=12962479; DOI=10.1021/bi0349266; RA Kroemer M., Merkel I., Schulz G.E.; RT "Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase."; RL Biochemistry 42:10560-10568(2003). CC -!- FUNCTION: Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate CC to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde CC (PubMed:12962479). Also catalyzes the dephosphorylation of phospho- CC serine in vitro (PubMed:25848029). {ECO:0000269|PubMed:12962479, CC ECO:0000269|PubMed:25848029}. 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:0000269|PubMed:12962479}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:11976494, ECO:0000269|PubMed:12962479}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11976494, CC ECO:0000269|PubMed:12962479}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.48 mM for L-rhamnulose 1-phosphate (at 37 degrees Celsius) CC {ECO:0000269|PubMed:12962479}; CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone CC phosphate from L-rhamnose: step 3/3. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11976494}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: Induced by L-rhamnose via the RhaR-RhaS regulatory cascade. CC Binding of the cAMP receptor protein (CRP) is required for full CC expression. {ECO:0000269|PubMed:10852886, ECO:0000269|PubMed:8230210}. CC -!- SIMILARITY: Belongs to the aldolase class II family. RhaD subfamily. CC {ECO:0000305}. 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; X60472; CAA43003.1; -; Genomic_DNA. DR EMBL; L19201; AAB03035.1; -; Genomic_DNA. DR EMBL; U00096; AAC76884.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77407.1; -; Genomic_DNA. DR PIR; C48649; C48649. DR RefSeq; NP_418338.1; NC_000913.3. DR RefSeq; WP_001179745.1; NZ_CP009789.1. DR PDB; 1GT7; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-274. DR PDB; 1OJR; X-ray; 1.35 A; A=1-274. DR PDB; 2UYU; X-ray; 1.96 A; A/E=1-274. DR PDB; 2UYV; X-ray; 2.20 A; A/B/C/D=1-274. DR PDB; 2V29; X-ray; 2.03 A; A/B=1-274. DR PDB; 2V2A; X-ray; 1.75 A; A=1-274. DR PDB; 2V2B; X-ray; 1.50 A; A=1-274. DR PDB; 2V9E; X-ray; 1.58 A; A/B=1-274. DR PDB; 2V9F; X-ray; 2.10 A; A=1-274. DR PDB; 2V9G; X-ray; 2.70 A; A/B/C/D=1-274. DR PDB; 2V9I; X-ray; 1.80 A; A/B=1-273. DR PDB; 2V9L; X-ray; 1.23 A; A=1-274. DR PDB; 2V9M; X-ray; 1.30 A; A/B=1-274. DR PDB; 2V9N; X-ray; 1.40 A; A/B/C/D=1-274. DR PDB; 2V9O; X-ray; 1.95 A; A/E=1-274. DR PDB; 9DGH; EM; 3.03 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-274. DR AlphaFoldDB; P32169; -. DR EMDB; EMD-46826; -. DR MDRepo; P32169; -. DR SMR; P32169; -. DR BioGRID; 4260676; 8. DR FunCoup; P32169; 124. DR IntAct; P32169; 7. DR STRING; 511145.b3902; -. DR DrugBank; DB03026; Phosphoglycolohydroxamic Acid. DR PaxDb; 511145-b3902; -. DR EnsemblBacteria; AAC76884; AAC76884; b3902. DR GeneID; 948401; -. DR KEGG; ecj:JW3873; -. DR KEGG; eco:b3902; -. DR KEGG; ecoc:C3026_21095; -. DR PATRIC; fig|1411691.4.peg.2804; -. DR EchoBASE; EB1812; -. DR eggNOG; COG0235; Bacteria. DR HOGENOM; CLU_076831_0_0_6; -. DR InParanoid; P32169; -. DR OMA; SHFMSHI; -. DR OrthoDB; 9784634at2; -. DR PhylomeDB; P32169; -. DR BioCyc; EcoCyc:RHAMNULPALDOL-MONOMER; -. DR BioCyc; MetaCyc:RHAMNULPALDOL-MONOMER; -. DR BRENDA; 4.1.2.19; 2026. DR SABIO-RK; P32169; -. DR UniPathway; UPA00541; UER00603. DR EvolutionaryTrace; P32169; -. DR PRO; PR:P32169; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P32169; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc. DR GO; GO:0008994; F:rhamnulose-1-phosphate aldolase activity; IDA:EcoCyc. DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central. DR GO; GO:0019301; P:rhamnose catabolic process; IMP:EcoCyc. DR CDD; cd00398; Aldolase_II; 1. DR FunFam; 3.40.225.10:FF:000006; Rhamnulose-1-phosphate aldolase; 1. DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1. DR HAMAP; MF_00770; RhaD; 1. DR InterPro; IPR050197; Aldolase_class_II_sugar_metab. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR InterPro; IPR036409; Aldolase_II/adducin_N_sf. DR InterPro; IPR013447; Rhamnulose-1-P_Aldolase. DR NCBIfam; NF002963; PRK03634.1; 1. DR NCBIfam; TIGR02624; rhamnu_1P_ald; 1. DR PANTHER; PTHR22789; FUCULOSE PHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR22789:SF16; RHAMNULOSE-1-PHOSPHATE ALDOLASE; 1. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1. DR PDBsum; 1GT7; -. DR PDBsum; 1OJR; -. DR PDBsum; 2UYU; -. DR PDBsum; 2UYV; -. DR PDBsum; 2V29; -. DR PDBsum; 2V2A; -. DR PDBsum; 2V2B; -. DR PDBsum; 2V9E; -. DR PDBsum; 2V9F; -. DR PDBsum; 2V9G; -. DR PDBsum; 2V9I; -. DR PDBsum; 2V9L; -. DR PDBsum; 2V9M; -. DR PDBsum; 2V9N; -. DR PDBsum; 2V9O; -. DR PDBsum; 9DGH; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Lyase; Metal-binding; Reference proteome; KW Rhamnose metabolism; Zinc. FT CHAIN 1..274 FT /note="Rhamnulose-1-phosphate aldolase" FT /id="PRO_0000209657" FT ACT_SITE 117 FT /evidence="ECO:0000269|PubMed:11976494, FT ECO:0000269|PubMed:12962479" FT BINDING 141 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:11976494, FT ECO:0000269|PubMed:12962479" FT BINDING 143 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:11976494, FT ECO:0000269|PubMed:12962479" FT BINDING 212 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:11976494, FT ECO:0000269|PubMed:12962479" FT MUTAGEN 28 FT /note="R->A,S: Severe loss of enzymatic activity." FT /evidence="ECO:0000269|PubMed:12962479" FT MUTAGEN 29 FT /note="N->A: Severe loss of enzymatic activity." FT /evidence="ECO:0000269|PubMed:12962479" FT MUTAGEN 117 FT /note="E->Q: Loss of enzymatic activity." FT /evidence="ECO:0000269|PubMed:12962479" FT MUTAGEN 171 FT /note="E->S,A,Q: Loss of enzymatic activity." FT /evidence="ECO:0000269|PubMed:12962479" FT MUTAGEN 192 FT /note="E->A: No effect on enzymatic activity." FT /evidence="ECO:0000269|PubMed:12962479" FT HELIX 4..6 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 8..22 FT /evidence="ECO:0007829|PDB:2V9L" FT STRAND 32..36 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 39..42 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 43..48 FT /evidence="ECO:0007829|PDB:2V9L" FT STRAND 54..57 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:2V9L" FT STRAND 69..74 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:2V9L" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 86..89 FT /evidence="ECO:0007829|PDB:2V9L" FT STRAND 90..95 FT /evidence="ECO:0007829|PDB:2V9L" FT STRAND 99..107 FT /evidence="ECO:0007829|PDB:2V9L" FT TURN 109..111 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 118..131 FT /evidence="ECO:0007829|PDB:2V9L" FT TURN 132..134 FT /evidence="ECO:0007829|PDB:2V9L" FT STRAND 138..142 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 145..150 FT /evidence="ECO:0007829|PDB:2V9L" FT TURN 151..153 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 158..167 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 172..175 FT /evidence="ECO:0007829|PDB:2V9L" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:2V9L" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 191..201 FT /evidence="ECO:0007829|PDB:2V9L" FT STRAND 205..209 FT /evidence="ECO:0007829|PDB:2V9L" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:2V9L" FT STRAND 213..220 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 221..243 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 256..263 FT /evidence="ECO:0007829|PDB:2V9L" FT HELIX 269..272 FT /evidence="ECO:0007829|PDB:2V9L" 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 //