LACD_STAAC
ID LACD_STAAC Reviewed; 326 AA.
AC Q5HE13;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=SACOL2183;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000046; AAW37059.1; -; Genomic_DNA.
DR RefSeq; WP_000047009.1; NC_002951.2.
DR PDB; 3MYP; X-ray; 2.99 A; A/B/C/D=1-326.
DR PDBsum; 3MYP; -.
DR AlphaFoldDB; Q5HE13; -.
DR SMR; Q5HE13; -.
DR MINT; Q5HE13; -.
DR EnsemblBacteria; AAW37059; AAW37059; SACOL2183.
DR KEGG; sac:SACOL2183; -.
DR HOGENOM; CLU_058971_0_1_9; -.
DR OMA; KDITRPS; -.
DR BRENDA; 4.1.2.40; 3352.
DR UniPathway; UPA00704; UER00716.
DR Proteomes; UP000000530; 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.
FT CHAIN 1..326
FT /note="Tagatose 1,6-diphosphate aldolase"
FT /id="PRO_0000203944"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:3MYP"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 46..60
FT /evidence="ECO:0007829|PDB:3MYP"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3MYP"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:3MYP"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:3MYP"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3MYP"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:3MYP"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:3MYP"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 136..155
FT /evidence="ECO:0007829|PDB:3MYP"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:3MYP"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 177..194
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:3MYP"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3MYP"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:3MYP"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:3MYP"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 293..300
FT /evidence="ECO:0007829|PDB:3MYP"
FT HELIX 303..318
FT /evidence="ECO:0007829|PDB:3MYP"
SQ SEQUENCE 326 AA; 36595 MW; 20766B1B841372C1 CRC64;
MSKSNQKIAS IEQLSNNEGI ISALAFDQRG ALKRMMAKHQ TEEPTVAQIE QLKVLVAEEL
TQYASSILLD PEYGLPASDA RNKDCGLLLA YEKTGYDVNA KGRLPDCLVE WSAKRLKEQG
ANAVKFLLYY DVDDAEEINI QKKAYIERIG SECVAEDIPF FLEVLTYDDN IPDNGSVEFA
KVKPRKVNEA MKLFSEPRFN VDVLKVEVPV NMKYVEGFAE GEVVYTKEEA AQHFKDQDAA
THLPYIYLSA GVSAELFQET LKFAHEAGAK FNGVLCGRAT WSGAVQVYIE QGEDAAREWL
RTTGFKNIDD LNKVLKDTAT SWKQRK
