RHAD_LISMF
ID RHAD_LISMF Reviewed; 273 AA.
AC Q71VR5;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=LMOf2365_2837;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(2004).
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 -!- 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; AE017262; AAT05601.1; -; Genomic_DNA.
DR RefSeq; WP_010959116.1; NC_002973.6.
DR AlphaFoldDB; Q71VR5; -.
DR SMR; Q71VR5; -.
DR KEGG; lmf:LMOf2365_2837; -.
DR HOGENOM; CLU_076831_0_0_9; -.
DR OMA; SHFMSHI; -.
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; ISS:JCVI.
DR GO; GO:0005996; P:monosaccharide metabolic process; ISS:JCVI.
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..273
FT /note="Rhamnulose-1-phosphate aldolase"
FT /id="PRO_0000209664"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00770"
SQ SEQUENCE 273 AA; 30545 MW; 1322AA1431AC18AE CRC64;
MTKDIMDAVF IKEMAKTTSN LYRLGWDERN GGNITYLLDE KEVVEYLDVK QIIRTIPMDF
DGKKLAGKYF LVTGSGKYFK NVEEAPAVNL GVIQVSEDGK AVHLLWGYTD SGLPTSELPA
HFMSHIARLS VDPENRVVMH CHATHLLAMT FTHELTEREF TRTLWQMCTE CLVVFPEGVG
IIPWLVPGTN EIGEATSEKM KENRLIVWPH HGIYGAGKSM DETFGLIETA EKAAEVYTIV
MSQGGIKQAI TDEQLKALGE RFGVEAKAGY LIN