ID R9IUN4_9FIRM Unreviewed; 275 AA.
AC R9IUN4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Rhamnulose-1-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00770};
DE EC=4.1.2.19 {ECO:0000256|HAMAP-Rule:MF_00770};
GN Name=rhaD {ECO:0000256|HAMAP-Rule:MF_00770};
GN ORFNames=C806_03269 {ECO:0000313|EMBL:EOS22657.1};
OS Lachnospiraceae bacterium 3-1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=397288 {ECO:0000313|EMBL:EOS22657.1, ECO:0000313|Proteomes:UP000014188};
RN [1] {ECO:0000313|EMBL:EOS22657.1, ECO:0000313|Proteomes:UP000014188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-1 {ECO:0000313|EMBL:EOS22657.1,
RC ECO:0000313|Proteomes:UP000014188};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 3-1.";
RL Submitted (APR-2013) 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:0000256|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:0000256|HAMAP-Rule:MF_00770};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00770};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00770};
CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone
CC phosphate from L-rhamnose: step 3/3. {ECO:0000256|HAMAP-Rule:MF_00770}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00770}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. RhaD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00770}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOS22657.1}.
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DR EMBL; ASST01000020; EOS22657.1; -; Genomic_DNA.
DR AlphaFoldDB; R9IUN4; -.
DR STRING; 397288.C806_03269; -.
DR PATRIC; fig|397288.3.peg.3542; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_076831_0_0_9; -.
DR OrthoDB; 9784634at2; -.
DR UniPathway; UPA00541; UER00603.
DR Proteomes; UP000014188; Unassembled WGS sequence.
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; Class II aldolase/adducin N-terminal domain; 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 PANTHER; PTHR22789:SF0; 3-OXO-TETRONATE 4-PHOSPHATE DECARBOXYLASE-RELATED; 1.
DR PANTHER; PTHR22789; FUCULOSE PHOSPHATE ALDOLASE; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00770};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00770};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00770};
KW Reference proteome {ECO:0000313|Proteomes:UP000014188};
KW Rhamnose metabolism {ECO:0000256|ARBA:ARBA00023308, ECO:0000256|HAMAP-
KW Rule:MF_00770}; Zinc {ECO:0000256|HAMAP-Rule:MF_00770}.
FT DOMAIN 10..238
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT ACT_SITE 116
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00770"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00770"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00770"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00770"
SQ SEQUENCE 275 AA; 31174 MW; EF363B8AA817D350 CRC64;
MSILDVKFVQ GFIRMCDDGW KQGWHERNGG NLSYRMKPEE VEEVKQFFSQ PGEWREIGTS
VPQLAGEYFM VTGSGKYFRN VILDPQDSAC IIELDEKGEN YRICWGMVNG GRPTSELPSH
LMNHEVKKAA SGGAHRVIYH AHTTNVIALT FVLPLKDEVF TRELWEMATE CPVVFPSGIG
VVGWMVPGGR DIAVATSELM KQYDVAVWAH HGMFCSGEDF DLTFGLMHTV EKSAEILVKM
LSMRPDKLQT ISPQNFRDLA KDFKVTLPDK FLYEK
//
