ID   LACD1_ENTFA             Reviewed;         325 AA.
AC   Q837X9;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Tagatose 1,6-diphosphate aldolase 1;
DE            EC=4.1.2.40;
DE   AltName: Full=D-tagatose-1,6-bisphosphate aldolase 1;
DE   AltName: Full=Tagatose-bisphosphate aldolase 1;
GN   Name=lacD1; Synonyms=lacD-1; OrderedLocusNames=EF_0696;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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; AE016830; AAO80517.1; -; Genomic_DNA.
DR   RefSeq; NP_814447.1; NC_004668.1.
DR   RefSeq; WP_002371479.1; NZ_KE136527.1.
DR   AlphaFoldDB; Q837X9; -.
DR   SMR; Q837X9; -.
DR   STRING; 226185.EF_0696; -.
DR   EnsemblBacteria; AAO80517; AAO80517; EF_0696.
DR   KEGG; efa:EF0696; -.
DR   PATRIC; fig|226185.45.peg.2638; -.
DR   eggNOG; COG3684; Bacteria.
DR   HOGENOM; CLU_058971_0_1_9; -.
DR   OMA; VAWLETT; -.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000001415; 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   3: Inferred from homology;
KW   Lactose metabolism; Lyase; Reference proteome.
FT   CHAIN           1..325
FT                   /note="Tagatose 1,6-diphosphate aldolase 1"
FT                   /id="PRO_0000203938"
SQ   SEQUENCE   325 AA;  36085 MW;  751531A7D74B2F50 CRC64;
     MKKISEQKRK HLENLVDDQG IIGALAIDQR GALKRMMGKY KEVTAQEISD FKVLVSRCLT
     PETSAILLDP EYGLAAAENR AQTSGLLLAY EKTGYDASTP GRLPDSLDVW SVKRLKEAGA
     DACKFLLYYD VDESEAINER KKAYIERIGS ECLAEEIPFF LEIVSYDANN SDSASKEYAK
     VKPHKVIEAM KEFSKDRYNV DVLKVEVPVN MNFVEGFGTE SLYSQDEAQA FFNMQSEATQ
     LPFIFLSAGV SATMFQETLK FAKKAGSSFN GVLCGRATWA DGVLPFVQQG AEAAVAWLET
     TGKTNVEELN QVLRESAVSV FEKIQ