ID A0A1G4VQ72_9FIRM Unreviewed; 271 AA.
AC A0A1G4VQ72;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN02910339_01471 {ECO:0000313|EMBL:SCX10179.1};
OS Lachnospiraceae bacterium YSD2013.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520828 {ECO:0000313|EMBL:SCX10179.1, ECO:0000313|Proteomes:UP000199278};
RN [1] {ECO:0000313|EMBL:SCX10179.1, ECO:0000313|Proteomes:UP000199278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSD2013 {ECO:0000313|EMBL:SCX10179.1,
RC ECO:0000313|Proteomes:UP000199278};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FMTX01000012; SCX10179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4VQ72; -.
DR STRING; 1520828.SAMN02910339_01471; -.
DR OrthoDB; 9784634at2; -.
DR UniPathway; UPA00541; UER00603.
DR Proteomes; UP000199278; 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:UP000199278};
KW Rhamnose metabolism {ECO:0000256|ARBA:ARBA00023308, ECO:0000256|HAMAP-
KW Rule:MF_00770}; Zinc {ECO:0000256|HAMAP-Rule:MF_00770}.
FT DOMAIN 9..237
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT ACT_SITE 115
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00770"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00770"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00770"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00770"
SQ SEQUENCE 271 AA; 30471 MW; F272D95FFAF40076 CRC64;
MITDAEFVKG FCNMCENGSK MGWHERNGGN LSYRIKGNEL ELIKAEIHES DAWREIGVSV
PRLAGEYFLV TGSGKYFANV AASPEENIGI IKIDEKGENY SIVWGFLNGA RPTSELPTHL
MNHEIKKMYT DGRYRVIYHA HPANLIALTF VLPLKDEVFT RELWETMTEC PVIFPKGVGV
VKWMVPGGRE IALATVEKMK EYDVTVWAHH GLFAAGEDFD LTFGLMHTVE KASEVLVKIL
SMTDARRQSI TTQDLISLGD AFGVRIPKKF L
//
