ID G7MBY3_9CLOT Unreviewed; 272 AA.
AC G7MBY3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=CDLVIII_0786 {ECO:0000313|EMBL:EHI97511.1};
OS Clostridium sp. DL-VIII.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI97511.1, ECO:0000313|Proteomes:UP000005106};
RN [1] {ECO:0000313|EMBL:EHI97511.1, ECO:0000313|Proteomes:UP000005106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHI97511.1,
RC ECO:0000313|Proteomes:UP000005106};
RX PubMed=23929491;
RA Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL Genome Announc. 1:e00605-e00613(2013).
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; CM001240; EHI97511.1; -; Genomic_DNA.
DR RefSeq; WP_009168193.1; NZ_CM001240.1.
DR AlphaFoldDB; G7MBY3; -.
DR STRING; 641107.CDLVIII_0786; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_076831_0_0_9; -.
DR UniPathway; UPA00541; UER00603.
DR Proteomes; UP000005106; 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; 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, ECO:0000313|EMBL:EHI97511.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00770};
KW Reference proteome {ECO:0000313|Proteomes:UP000005106};
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 272 AA; 30309 MW; 1BA849430E365467 CRC64;
MAIEDMKFIE NFKKITNDAW LKGWHERNGG NITYRLTEDE VVAIGGFINE DSKYTPIGVT
VKNLANEYFL VTGSGKFIRN MEISLEENAG IIKIDEKGEN YKIVWGLKNE AKPTSELDSH
LMSHSIKVEK TNGAHRVIMH SHTTNVIALT FVLPLDGVVF TRELWEMATE CPVVFPSGIG
VVPWMVPGGA AIAEVTGELM KRHDVVIWAH HGMFCSGETL DLTFGLMDTV EKSAEILVKV
LSMGGKKQTI TSQNFRDLAK DFNVTISEDY LG
//
