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LACD2_STRMU
ID   LACD2_STRMU             Reviewed;         329 AA.
AC   Q8DWE5;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Tagatose 1,6-diphosphate aldolase 2;
DE            EC=4.1.2.40;
DE   AltName: Full=D-tagatose-1,6-bisphosphate aldolase 2;
DE   AltName: Full=Tagatose-bisphosphate aldolase 2;
GN   Name=lacD2; OrderedLocusNames=SMU_116;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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   -!- 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.
CC   -!- SIMILARITY: Belongs to the aldolase LacD family. {ECO:0000305}.
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DR   EMBL; AE014133; AAN57897.1; -; Genomic_DNA.
DR   RefSeq; NP_720591.1; NC_004350.2.
DR   RefSeq; WP_002265910.1; NC_004350.2.
DR   PDB; 3IV3; X-ray; 1.80 A; A=1-329.
DR   PDBsum; 3IV3; -.
DR   AlphaFoldDB; Q8DWE5; -.
DR   SMR; Q8DWE5; -.
DR   STRING; 210007.SMU_116; -.
DR   EnsemblBacteria; AAN57897; AAN57897; SMU_116.
DR   KEGG; smu:SMU_116; -.
DR   eggNOG; COG3684; Bacteria.
DR   HOGENOM; CLU_058971_0_1_9; -.
DR   OMA; KDITRPS; -.
DR   PhylomeDB; Q8DWE5; -.
DR   UniPathway; UPA00704; UER00716.
DR   EvolutionaryTrace; Q8DWE5; -.
DR   Proteomes; UP000002512; Chromosome.
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; -; 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   Pfam; PF01791; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
DR   TIGRFAMs; TIGR01232; lacD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Lactose metabolism; Lyase; Reference proteome.
FT   CHAIN           1..329
FT                   /note="Tagatose 1,6-diphosphate aldolase 2"
FT                   /id="PRO_0000203958"
FT   HELIX           5..13
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   STRAND          21..26
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           30..37
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   TURN            38..40
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           46..60
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   STRAND          64..69
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           75..79
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   STRAND          86..90
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           113..118
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   STRAND          122..130
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           136..156
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   STRAND          160..166
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           177..180
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           183..194
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   STRAND          202..206
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   TURN            216..218
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           227..239
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   STRAND          245..248
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           254..267
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   STRAND          273..276
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           278..281
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           284..291
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           293..300
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           303..318
FT                   /evidence="ECO:0007829|PDB:3IV3"
FT   HELIX           322..324
FT                   /evidence="ECO:0007829|PDB:3IV3"
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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