ID   LACD_LISIN              Reviewed;         338 AA.
AC   Q92EB7;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Tagatose 1,6-diphosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00734};
DE            EC=4.1.2.40 {ECO:0000255|HAMAP-Rule:MF_00734};
DE   AltName: Full=D-tagatose-1,6-bisphosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00734};
DE   AltName: Full=Tagatose-bisphosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00734};
GN   Name=lacD {ECO:0000255|HAMAP-Rule:MF_00734}; OrderedLocusNames=lin0543;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00734}.
CC   -!- SIMILARITY: Belongs to the aldolase LacD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00734}.
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DR   EMBL; AL596165; CAC95775.1; -; Genomic_DNA.
DR   PIR; AG1500; AG1500.
DR   RefSeq; WP_003770662.1; NC_003212.1.
DR   AlphaFoldDB; Q92EB7; -.
DR   SMR; Q92EB7; -.
DR   STRING; 272626.lin0543; -.
DR   EnsemblBacteria; CAC95775; CAC95775; CAC95775.
DR   GeneID; 61169572; -.
DR   KEGG; lin:lin0543; -.
DR   eggNOG; COG3684; Bacteria.
DR   HOGENOM; CLU_058971_0_1_9; -.
DR   OMA; HEKVIVE; -.
DR   OrthoDB; 1560751at2; -.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000002513; 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.
PE   3: Inferred from homology;
KW   Lactose metabolism; Lyase.
FT   CHAIN           1..338
FT                   /note="Tagatose 1,6-diphosphate aldolase"
FT                   /id="PRO_0000203941"
SQ   SEQUENCE   338 AA;  37711 MW;  81216267CA4A2915 CRC64;
     MVQITKGKFD GLQRLSNDKG VIAALAIDQR GSLKKMIQQA KGTENKKDVE DFKQLVSEEL
     TPYASAILLD LEYGTPAIKA RHEGSGLLTS YEKTGYDATT PGKLPDLIED LSALRIKENG
     GDAVKILVYY DPDEPAEINE IKYAFLERIG AECRAVDIPF FLEPITYDAK VTDSGSLEYA
     KLKPAKVKAS IKEFSKPRYG VDVLKLEVPV NFKYVEGFAE GEVAYTQDEA ARHFEECSDL
     SPLPFIYLSA GVTSEMFHKT IQFANQHNVQ YSGVLCGRAT WADGIEVYGK QGDDALREWL
     RTQGKENITS LDKLLDEGAV PWWTKYGSFE DVHVVEKQ