ID A0A1I4S8Y1_9HYPH Unreviewed; 281 AA.
AC A0A1I4S8Y1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 08-OCT-2025, entry version 31.
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=CXZ10_11570 {ECO:0000313|EMBL:PKR88759.1};
OS Pleomorphomonas diazotrophica.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Pleomorphomonadaceae; Pleomorphomonas.
OX NCBI_TaxID=1166257 {ECO:0000313|EMBL:PKR88759.1, ECO:0000313|Proteomes:UP000233491};
RN [1] {ECO:0000313|EMBL:PKR88759.1, ECO:0000313|Proteomes:UP000233491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R5-392 {ECO:0000313|EMBL:PKR88759.1,
RC ECO:0000313|Proteomes:UP000233491};
RA Esquivel-Elizondo S., Krajmalnik-Brown R.;
RT "Anaerobic carbon monoxide metabolism by Pleomorphomonas carboxyditropha
RT sp. nov., a new mesophilic hydrogenogenic carboxidotroph.";
RL Submitted (DEC-2017) 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:PKR88759.1}.
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DR EMBL; PJNW01000009; PKR88759.1; -; Genomic_DNA.
DR RefSeq; WP_101289417.1; NZ_FOUQ01000003.1.
DR AlphaFoldDB; A0A1I4S8Y1; -.
DR OrthoDB; 9784634at2; -.
DR UniPathway; UPA00541; UER00603.
DR Proteomes; UP000233491; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0019323; P:pentose catabolic process; IEA:TreeGrafter.
DR GO; GO:0019301; P:rhamnose catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR HAMAP; MF_00770; RhaD; 1.
DR InterPro; IPR050197; Aldolase_class_II_sugar_metab.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR013447; Rhamnulose-1-P_Aldolase.
DR NCBIfam; NF002963; PRK03634.1; 1.
DR PANTHER; PTHR22789; FUCULOSE PHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR22789:SF16; RHAMNULOSE-1-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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00770};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00770}; Reference proteome {ECO:0000313|Proteomes:UP000233491};
KW Rhamnose metabolism {ECO:0000256|ARBA:ARBA00023308, ECO:0000256|HAMAP-
KW Rule:MF_00770};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00770}.
FT DOMAIN 12..239
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT ACT_SITE 117
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 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00770"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00770"
SQ SEQUENCE 281 AA; 30699 MW; D72C5B86780B4549 CRC64;
MTANMIDSWF VKAMVKATTD CWDKGWDERN GGNISLRLTD DDLAPYLAGI REPRRLPMTE
PLPAIAGQSY IVTGTGKFFR NVQLDPENNL GVVRVGADGS FLEVLWGYRD GGGPTSEFSS
HFKGHIARQN ATNGSDRVVL HCHATNLIAL TYVLQWNDAN VTRALWEGST ECLVVFPDGV
GTMPWLVPGT DQMGDATARL LAKRPLVLWP FHGVFGVGPT LDDAFGLIDT AEKAAEILVK
VLSMGGPRQT MSTQDLIDLA ARFKVVPQPE AMALDGWRLA D
//
