ID Q1J4Q4_STRPF Unreviewed; 327 AA.
AC Q1J4Q4;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
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=lacD {ECO:0000256|HAMAP-Rule:MF_00734};
GN Synonyms=lacD2 {ECO:0000313|EMBL:ABF38682.1};
GN OrderedLocusNames=MGAS10750_Spy1732 {ECO:0000313|EMBL:ABF38682.1};
OS Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370554 {ECO:0000313|EMBL:ABF38682.1, ECO:0000313|Proteomes:UP000002434};
RN [1] {ECO:0000313|EMBL:ABF38682.1, ECO:0000313|Proteomes:UP000002434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS10750 {ECO:0000313|EMBL:ABF38682.1,
RC ECO:0000313|Proteomes:UP000002434};
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000262; ABF38682.1; -; Genomic_DNA.
DR RefSeq; WP_011529001.1; NC_008024.1.
DR AlphaFoldDB; Q1J4Q4; -.
DR KEGG; spi:MGAS10750_Spy1732; -.
DR HOGENOM; CLU_058971_0_1_9; -.
DR UniPathway; UPA00704; UER00716.
DR Proteomes; UP000002434; 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}.
SQ SEQUENCE 327 AA; 36621 MW; A07775CDDED84DC3 CRC64;
MTITLTENKR KSMEKLSIDG VISALAFDQR GALKRMMAQH QTKEPTVEQI EELKSLVSEE
LTPFASSILL DPEYGLPASR VRSEEAGLLL AYEKTGYDAT TTSRLPDCLD VWSAKRIKEA
GAEAVKFLLY YDIDGDQDVN EQKKAYIERI GSECRAEDIP FYLEILTYDE KIADNASPEF
AKVKAHKVNE AMKVFSKERF GVDVLKVEVP VNMKFVEGFA DGEVLFTKEE AAQAFRDQEA
STDLPYIYLS AGVSAKLFQD TLEFAAESGA KFNGVLCGRA TWAGSVKVYI EEGPQAAREW
LRTEGFKNID ELNKVLDKTA SPWTEKM
//
