ID A8AYE2_STRGC Unreviewed; 323 AA.
AC A8AYE2;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
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-1 {ECO:0000313|EMBL:ABV09133.1};
GN Synonyms=lacD {ECO:0000256|HAMAP-Rule:MF_00734};
GN OrderedLocusNames=SGO_1523 {ECO:0000313|EMBL:ABV09133.1};
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705 {ECO:0000313|EMBL:ABV09133.1, ECO:0000313|Proteomes:UP000001131};
RN [1] {ECO:0000313|EMBL:ABV09133.1, ECO:0000313|Proteomes:UP000001131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288
RC {ECO:0000313|Proteomes:UP000001131};
RX PubMed=17720781; DOI=10.1128/JB.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(2007).
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; CP000725; ABV09133.1; -; Genomic_DNA.
DR RefSeq; WP_012130595.1; NC_009785.1.
DR AlphaFoldDB; A8AYE2; -.
DR STRING; 467705.SGO_1523; -.
DR KEGG; sgo:SGO_1523; -.
DR eggNOG; COG3684; Bacteria.
DR HOGENOM; CLU_058971_0_1_9; -.
DR UniPathway; UPA00704; UER00716.
DR Proteomes; UP000001131; 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:UP000001131}.
SQ SEQUENCE 323 AA; 35880 MW; 01A4E30787CB728E CRC64;
MALTEQKRAR LEKLSDENGI ISALAFDQRG ALKRLMAQYQ TEEPTVAQME ELKVLVADEL
TKYASSMLLD PEYGLPATKA LDANAGLLLA YEKTGYDTTS TKRLPDCLDV WSAKRIKEQG
ADAVKFLLYY DVDSSDELNQ QKQAYIERIG SECVAEDIPF FLEILAYDEK IADAGSAEYA
KVKPHKVIGA MKVFSDPRFN IDVLKVEVPV NVKYVEGFGD GEIVHTREEA AAFFKAQDEA
TNLPYIYLSA GVSAKLFQET LVFAHESGAN FNGVLCGRAT WAGSVEAYIK DGEAAAREWL
RTEGRQNIEE LNQVLKSSAT SWK
//
