LACD1_STRP1
ID LACD1_STRP1 Reviewed; 325 AA.
AC P63703; Q48XB2; Q99YH3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 119.
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=SPy_1704, M5005_Spy1395;
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; AAK34454.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ52013.1; -; Genomic_DNA.
DR RefSeq; NP_269733.1; NC_002737.2.
DR PDB; 3MYO; X-ray; 2.50 A; A/B=1-325.
DR PDBsum; 3MYO; -.
DR AlphaFoldDB; P63703; -.
DR SMR; P63703; -.
DR IntAct; P63703; 1.
DR MINT; P63703; -.
DR STRING; 1314.HKU360_01449; -.
DR PaxDb; P63703; -.
DR EnsemblBacteria; AAK34454; AAK34454; SPy_1704.
DR KEGG; spy:SPy_1704; -.
DR KEGG; spz:M5005_Spy1395; -.
DR PATRIC; fig|160490.10.peg.1482; -.
DR HOGENOM; CLU_058971_0_1_9; -.
DR OMA; VAWLETT; -.
DR UniPathway; UPA00704; UER00716.
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..325
FT /note="Tagatose 1,6-diphosphate aldolase 1"
FT /id="PRO_0000203961"
FT HELIX 5..13
FT /evidence="ECO:0007829|PDB:3MYO"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:3MYO"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:3MYO"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3MYO"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:3MYO"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:3MYO"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:3MYO"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 135..155
FT /evidence="ECO:0007829|PDB:3MYO"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:3MYO"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:3MYO"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:3MYO"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 292..300
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 302..317
FT /evidence="ECO:0007829|PDB:3MYO"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:3MYO"
SQ SEQUENCE 325 AA; 36011 MW; 7B3A1B69AF3C471E CRC64;
MTITANKRHY LEKVSHQGII SALAFDQRGA LKQMMAAHQE GEATVTQIET LKVLVSEELT
PYASSILLDP EYGLLATKVR ANQTGLLLAY EKTGYDATTT SRLPDCLVEW SVKRLKAAGA
DAIKFLLYYD VDGDEQINLQ KQAYIERIGS ECTAEDIPFF LELLSYDERI SDNNSAAYAK
LKPHKVNGAM SVFSDKRFGV DVLKVEVPVN MAYVEGFTEG EVHYSQAEAI KAFQDQEAAS
HLPYIYLSAG VSAKLFQETL YFAAAAGAQF SGVLCGRATW AGSVPVYITK GEDEARKWLC
TEGFQNIDEL NRVLEETASP WTEKI
