ID   LACD_STAHJ              Reviewed;         325 AA.
AC   Q4L871;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 116.
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=SH0845;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04154.1; -; Genomic_DNA.
DR   RefSeq; WP_011275158.1; NC_007168.1.
DR   AlphaFoldDB; Q4L871; -.
DR   SMR; Q4L871; -.
DR   STRING; 279808.SH0845; -.
DR   EnsemblBacteria; BAE04154; BAE04154; SH0845.
DR   GeneID; 58106727; -.
DR   KEGG; sha:SH0845; -.
DR   eggNOG; COG3684; Bacteria.
DR   HOGENOM; CLU_058971_0_1_9; -.
DR   OMA; KDITRPS; -.
DR   OrthoDB; 1560751at2; -.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000000543; 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.
FT   CHAIN           1..325
FT                   /note="Tagatose 1,6-diphosphate aldolase"
FT                   /id="PRO_0000203953"
SQ   SEQUENCE   325 AA;  36569 MW;  DCE841BB6C1256D3 CRC64;
     MTKSQQKLAS IEQLSNQDGI ISALAFDQRG ALKRMMAEHQ TEPPTVEQIE QLKVLVSEEL
     TQYASSILLD PEYGLPASDA RNKECGLLLA YEKTGYDVNA KGRLPDCLVE WSAKRLKEQG
     ANAVKFLLYY DVDDSEEINI QKKAYIERIG SECVAEDIPF FLEVLTYDDN IPDNKSAEFA
     KVKPRKVNEA MKLFSEDRFN VDVLKVEVPV NMNFVEGFTE GEVVYTKEEA AQHFRDQEAA
     THLPYIYLSA GVSAELFQET LTFAHDAGAH FNGVLCGRAT WSGAVKVYIE QGEQAAREWL
     RTTGYKNIDD LNKVLKTTAT SWKAK