LACD2_STRP1
ID LACD2_STRP1 Reviewed; 327 AA.
AC P63705; Q48WM2; Q99Y15;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 117.
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; Synonyms=lacD.2; OrderedLocusNames=SPy_1919, M5005_Spy1635;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(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 -!- 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; AE004092; AAK34623.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ52253.1; -; Genomic_DNA.
DR RefSeq; NP_269902.1; NC_002737.2.
DR PDB; 3JRK; X-ray; 1.97 A; A/B/C/D/E/F/G/H=6-327.
DR PDB; 3MHF; X-ray; 1.87 A; A/B/C/D=2-327.
DR PDB; 3MHG; X-ray; 1.92 A; A/B/C/D=2-327.
DR PDB; 5F2G; X-ray; 1.92 A; A/B/C/D=1-327.
DR PDB; 5F2I; X-ray; 1.95 A; A/B/C/D=1-327.
DR PDB; 5F2L; X-ray; 1.75 A; A/B/C/D=1-327.
DR PDB; 5F2M; X-ray; 1.92 A; A/B/C/D=1-327.
DR PDB; 5F4S; X-ray; 1.72 A; A/B/C/D=1-327.
DR PDB; 5F4W; X-ray; 1.66 A; A/B/C/D=1-327.
DR PDB; 5FF7; X-ray; 2.09 A; A/B/C/D=1-327.
DR PDBsum; 3JRK; -.
DR PDBsum; 3MHF; -.
DR PDBsum; 3MHG; -.
DR PDBsum; 5F2G; -.
DR PDBsum; 5F2I; -.
DR PDBsum; 5F2L; -.
DR PDBsum; 5F2M; -.
DR PDBsum; 5F4S; -.
DR PDBsum; 5F4W; -.
DR PDBsum; 5FF7; -.
DR AlphaFoldDB; P63705; -.
DR SMR; P63705; -.
DR STRING; 1314.HKU360_01758; -.
DR PaxDb; P63705; -.
DR EnsemblBacteria; AAK34623; AAK34623; SPy_1919.
DR KEGG; spy:SPy_1919; -.
DR KEGG; spz:M5005_Spy1635; -.
DR PATRIC; fig|160490.10.peg.1668; -.
DR HOGENOM; CLU_058971_0_1_9; -.
DR OMA; KDITRPS; -.
DR UniPathway; UPA00704; UER00716.
DR EvolutionaryTrace; P63705; -.
DR Proteomes; UP000000750; 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..327
FT /note="Tagatose 1,6-diphosphate aldolase 2"
FT /id="PRO_0000203965"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:5F4W"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:5F4W"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:5F4W"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:5F4W"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:5F4W"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:5F4W"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 137..157
FT /evidence="ECO:0007829|PDB:5F4W"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 178..195
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:5F4W"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:5F4W"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 228..239
FT /evidence="ECO:0007829|PDB:5F4W"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:5F4W"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 285..292
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 304..319
FT /evidence="ECO:0007829|PDB:5F4W"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:5F4W"
SQ SEQUENCE 327 AA; 36577 MW; 4E179B441A90543E CRC64;
MTITLTENKR KSMEKLSVDG VISALAFDQR GALKRMMAQH QTKEPTVEQI EELKSLVSEE
LTPFASSILL DPEYGLPASR VRSEEAGLLL AYEKTGYDAT TTSRLPDCLD VWSAKRIKEA
GAEAVKFLLY YDIDGDQDVN EQKKAYIERI GSECRAEDIP FYLEILTYDE KIADNASPEF
AKVKAHKVNE AMKVFSKERF GVDVLKVEVP VNMKFVEGFA DGEVLFTKEE AAQAFRDQEA
STDLPYIYLS AGVSAKLFQD TLVFAAESGA KFNGVLCGRA TWAGSVKVYI EEGPQAAREW
LRTEGFKNID ELNKVLDKTA SPWTEKM
