ID C9A630_ENTCA Unreviewed; 274 AA.
AC C9A630;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=ECBG_00210 {ECO:0000313|EMBL:EEV37941.1};
OS Enterococcus casseliflavus EC20.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=565655 {ECO:0000313|EMBL:EEV37941.1, ECO:0000313|Proteomes:UP000012675};
RN [1] {ECO:0000313|EMBL:EEV37941.1, ECO:0000313|Proteomes:UP000012675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC20 {ECO:0000313|EMBL:EEV37941.1,
RC ECO:0000313|Proteomes:UP000012675};
RG The Broad Institute Genome Sequencing Platform;
RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Gilmore M., Manson J., Palmer K., Carniol K.,
RA Lander E., Nusbaum C., Galagan J., Birren B.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEV37941.1, ECO:0000313|Proteomes:UP000012675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC20 {ECO:0000313|EMBL:EEV37941.1,
RC ECO:0000313|Proteomes:UP000012675};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Russ C., Feldgarden M., Gilmore M., Manson J., Palmer K., Carniol K.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus casseliflavus EC20 (899205).";
RL Submitted (MAR-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}.
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DR EMBL; CP004856; EEV37941.1; -; Genomic_DNA.
DR RefSeq; WP_005234418.1; NZ_AKCC01000001.1.
DR AlphaFoldDB; C9A630; -.
DR GeneID; 15141427; -.
DR KEGG; ecas:ECBG_00210; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_076831_0_0_9; -.
DR UniPathway; UPA00541; UER00603.
DR Proteomes; UP000012675; 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 NCBIfam; TIGR02624; rhamnu_1P_ald; 1.
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:UP000012675};
KW Rhamnose metabolism {ECO:0000256|ARBA:ARBA00023308, ECO:0000256|HAMAP-
KW Rule:MF_00770}; Zinc {ECO:0000256|HAMAP-Rule:MF_00770}.
FT DOMAIN 13..239
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT ACT_SITE 118
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 274 AA; 30729 MW; 08451CA631B776AA CRC64;
MKKIDILQAN FVQEMMETTA NLYRLGWDER NGGNISYLLT EEEILPFIDP QSVLREIPMI
FDATALAGKY FIVTGSGKYF KNVAAHPAEN LGVIRVKEDG QTLELLWGLE NGAVPTSELP
SHFMSHIARL SVDPENRIIM HNHASHLLAM SFTHELDERS FTRTLWQMCT ECLVVFPEGV
SIIPWMVPGT NEIGEATAAK MKETRLVLWP QHGIYGAGKD MDEVFGLIET AEKAAEVYTY
VKAQGPILQT ITDENLKKLA DAFKVTPRAG YLEV
//
