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Database: UniProt
Entry: Q1LZ67_STRMU
LinkDB: Q1LZ67_STRMU
Original site: Q1LZ67_STRMU 
ID   Q1LZ67_STRMU            Unreviewed;       329 AA.
AC   Q1LZ67;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Tagatose 1,6-diphosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00734};
DE            EC=4.1.2.40 {ECO:0000256|HAMAP-Rule:MF_00734};
DE   AltName: Full=D-tagatose-1,6-bisphosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00734};
DE   AltName: Full=Tagatose-bisphosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00734};
GN   Name=tdpA {ECO:0000313|EMBL:DAA01809.1};
GN   Synonyms=lacD {ECO:0000256|HAMAP-Rule:MF_00734};
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007 {ECO:0000313|EMBL:DAA01809.1};
RN   [1] {ECO:0000313|EMBL:DAA01809.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UA159 {ECO:0000313|EMBL:DAA01809.1};
RX   PubMed=11750824; DOI=10.1111/j.1574-6968.2001.tb10969.x;
RA   Wen Z.T., Browngardt C., Burne R.A.;
RT   "Characterization of two operons that encode components of fructose-
RT   specific enzyme II of the sugar:phosphotransferase system of Streptococcus
RT   mutans.";
RL   FEMS Microbiol. Lett. 205:337-342(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-tagatofuranose 1,6-bisphosphate = D-glyceraldehyde 3-
CC         phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:22948,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:58694, ChEBI:CHEBI:59776; EC=4.1.2.40;
CC         Evidence={ECO:0000256|ARBA:ARBA00000567, ECO:0000256|HAMAP-
CC         Rule:MF_00734};
CC   -!- PATHWAY: Carbohydrate metabolism; D-tagatose 6-phosphate degradation;
CC       D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-
CC       phosphate: step 2/2. {ECO:0000256|ARBA:ARBA00005191, ECO:0000256|HAMAP-
CC       Rule:MF_00734}.
CC   -!- SIMILARITY: Belongs to the aldolase LacD family.
CC       {ECO:0000256|ARBA:ARBA00008679, ECO:0000256|HAMAP-Rule:MF_00734}.
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DR   EMBL; BK000030; DAA01809.1; -; Genomic_DNA.
DR   RefSeq; NP_720591.1; NC_004350.2.
DR   RefSeq; WP_002265910.1; NC_004350.2.
DR   AlphaFoldDB; Q1LZ67; -.
DR   SMR; Q1LZ67; -.
DR   PATRIC; fig|210007.7.peg.98; -.
DR   OrthoDB; 106309at2; -.
DR   PhylomeDB; Q1LZ67; -.
DR   UniPathway; UPA00704; UER00716.
DR   GO; GO:0009024; F:tagatose-6-phosphate kinase activity; IEA:InterPro.
DR   GO; GO:0009025; F:tagatose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:2001059; P:D-tagatose 6-phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019512; P:lactose catabolic process via tagatose-6-phosphate; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00734; LacD; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR005927; Tag_1.6-dipho_adolase.
DR   NCBIfam; TIGR01232; lacD; 1.
DR   PANTHER; PTHR39340; SULFOFRUCTOSEPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR39340:SF1; SULFOFRUCTOSEPHOSPHATE ALDOLASE; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Lactose metabolism {ECO:0000256|ARBA:ARBA00022736, ECO:0000256|HAMAP-
KW   Rule:MF_00734};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00734}.
SQ   SEQUENCE   329 AA;  36558 MW;  C748440C78C1B77B CRC64;
     MILSQQKYNY LAKVSDSNGV ISALAFDQRG ALKCLMAQYQ MKEPTVAQME ELKVLVSEEL
     TPYASSILLD PEYGLPAAQA RDREAGLLLA YEKTGYDANT TSRLPDCLVD WSIKRLKEAG
     ADAVKFLLYY DVDGDPQVNV QKQAYIERIG SECQAEDIPF FLEILTYDET ISNNSSVEFA
     KVKVHKVNDA MKVFSAERFG IDVLKVEVPV NMVYVEGFAE GEVVYSKEEA AQAFREQEAS
     TDLPYIYLSA GVSAELFQET LVFAHKAGAK FNGVLCGRAT WAGSVQVYME EGKEAARQWL
     RTSGLQNINE LNKVLKTTAS PWTEKVSVG
//
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