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