ID B9DSS4_STRU0 Unreviewed; 326 AA.
AC B9DSS4;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Tagatose 1,6-diphosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00734};
DE EC=4.1.2.40 {ECO:0000256|HAMAP-Rule:MF_00734};
DE AltName: Full=D-tagatose-1,6-bisphosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00734};
DE AltName: Full=Tagatose-bisphosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00734};
GN Name=lacD3 {ECO:0000313|EMBL:CAR40396.1};
GN Synonyms=lacD {ECO:0000256|HAMAP-Rule:MF_00734};
GN OrderedLocusNames=SUB0040 {ECO:0000313|EMBL:CAR40396.1};
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495 {ECO:0000313|EMBL:CAR40396.1, ECO:0000313|Proteomes:UP000000449};
RN [1] {ECO:0000313|Proteomes:UP000000449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J {ECO:0000313|Proteomes:UP000000449};
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
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:0000256|ARBA:ARBA00000567, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00005191, ECO:0000256|HAMAP-
CC Rule:MF_00734}.
CC -!- SIMILARITY: Belongs to the aldolase LacD family.
CC {ECO:0000256|ARBA:ARBA00008679, ECO:0000256|HAMAP-Rule:MF_00734}.
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DR EMBL; AM946015; CAR40396.1; -; Genomic_DNA.
DR RefSeq; WP_012657608.1; NC_012004.1.
DR AlphaFoldDB; B9DSS4; -.
DR STRING; 218495.SUB0040; -.
DR KEGG; sub:SUB0040; -.
DR eggNOG; COG3684; Bacteria.
DR HOGENOM; CLU_058971_0_1_9; -.
DR OrthoDB; 106309at2; -.
DR UniPathway; UPA00704; UER00716.
DR Proteomes; UP000000449; 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; Aldolase class I; 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 NCBIfam; TIGR01232; lacD; 1.
DR PANTHER; PTHR39340; SULFOFRUCTOSEPHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR39340:SF1; SULFOFRUCTOSEPHOSPHATE ALDOLASE; 1.
DR Pfam; PF01791; DeoC; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Lactose metabolism {ECO:0000256|ARBA:ARBA00022736, ECO:0000256|HAMAP-
KW Rule:MF_00734};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00734};
KW Reference proteome {ECO:0000313|Proteomes:UP000000449}.
SQ SEQUENCE 326 AA; 36335 MW; 40213866A13ED5B3 CRC64;
MYQITDEKRR KLEKLSHNGI ISALAFDQRG ALKRMMAAHQ STEPTVEQIE ELKVMVSEEL
TPYASSILLD PEYGLPAVKV KDEQAGLLLA YEKTGYDATT TSRLPDCLVE WSAKRLKEAG
ADAVKFLLYY DVDGDQAIND QKKAYIERIG SECQAEDIPF FLEVLTYDEK IADNGSLEFA
KVKAHKVNEA MKVFSDERFG IDVLKVEVPV NMNYVEGFAE GEAVFTREEA AQAFKEQEAA
SHLPYIYLSA GVSAELFQET LVFAAESGAK FNGVLCGRAT WAGSVPVYIG QGQEAARQWL
RTEGFNNIDG LNKVIERTAS SWELKL
//