RHAD_ECOLU
ID RHAD_ECOLU Reviewed; 274 AA.
AC B7NFK0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=ECUMN_4430;
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928163; CAR15557.1; -; Genomic_DNA.
DR RefSeq; WP_001179732.1; NC_011751.1.
DR RefSeq; YP_002415046.1; NC_011751.1.
DR AlphaFoldDB; B7NFK0; -.
DR SMR; B7NFK0; -.
DR STRING; 585056.ECUMN_4430; -.
DR EnsemblBacteria; CAR15557; CAR15557; ECUMN_4430.
DR KEGG; eum:ECUMN_4430; -.
DR PATRIC; fig|585056.7.peg.4599; -.
DR HOGENOM; CLU_076831_0_0_6; -.
DR OMA; SHFMSHI; -.
DR UniPathway; UPA00541; UER00603.
DR Proteomes; UP000007097; Chromosome.
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_1000193725"
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; 30097 MW; D417DA68748F39A8 CRC64;
MQNITQSWFV QGMIKATTDA WLKGWDERNG GNLTLRLDDA DIAPYHDNFH AQPRYIPLSQ
PMPLLANTPF IVTGSGKFFR NVQLDPAANL GVVKVDSDGA GYHILWGLTH EAVPTSELPA
HFLSHCERIK ATNGKDRVIM HCHATNLIAL TYVLENDTAV FTRQLWEGST ECLVVFPDGV
GILPWMVPGT DEIGQATAQE MQKHSLVLWP FHGVFGSGPT LDETFGLIDT AEKSAQVLVK
VYSMGGMKQT ISREELIALG QRFGVTPLAS ALAL