RHAD_ECO7I
ID RHAD_ECO7I Reviewed; 274 AA.
AC B7NUA6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=ECIAI39_3095;
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI39 / 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}.
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; CU928164; CAR19214.1; -; Genomic_DNA.
DR RefSeq; WP_001179757.1; NC_011750.1.
DR RefSeq; YP_002409025.1; NC_011750.1.
DR AlphaFoldDB; B7NUA6; -.
DR SMR; B7NUA6; -.
DR STRING; 585057.ECIAI39_3095; -.
DR EnsemblBacteria; CAR19214; CAR19214; ECIAI39_3095.
DR KEGG; ect:ECIAI39_3095; -.
DR PATRIC; fig|585057.6.peg.3210; -.
DR HOGENOM; CLU_076831_0_0_6; -.
DR OMA; SHFMSHI; -.
DR UniPathway; UPA00541; UER00603.
DR Proteomes; UP000000749; 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_1000193727"
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; 30004 MW; 970704779BDB244E CRC64;
MQNITQSWFV QGMIKATTDA WLKGWDERNG GNLTLRLDDA DIAPYHGNFH AQPRYIPLSQ
PMPLLANTPF IVTGSGKFFR NVQLDPAANL GVVKVDSDGA GYHILWGLTN EAVPTSELPA
HFLSHCERIK ATNGKDRVIM HCHATNLIAL TYVLENDTAV FTRQLWEGST ECLVVFPDGV
GILPWMVPGT DEIGQATAQE MQKHSLVLWP FHGVFSSGPT LDETFGLIDT AEKSAQVLVK
GYSMGGMKQT ISREELIALG QRFGVTPLAS ALAL