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Database: UniProt
Entry: F5VX15_STROR
LinkDB: F5VX15_STROR
Original site: F5VX15_STROR 
ID   F5VX15_STROR            Unreviewed;       326 AA.
AC   F5VX15;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
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   ECO:0000313|EMBL:EGL85104.1};
GN   ORFNames=HMPREF9968_0277 {ECO:0000313|EMBL:EGL85104.1};
OS   Streptococcus oralis SK255.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1005704 {ECO:0000313|EMBL:EGL85104.1, ECO:0000313|Proteomes:UP000003695};
RN   [1] {ECO:0000313|EMBL:EGL85104.1, ECO:0000313|Proteomes:UP000003695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK255 {ECO:0000313|EMBL:EGL85104.1,
RC   ECO:0000313|Proteomes:UP000003695};
RA   Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGL85104.1}.
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DR   EMBL; AFNM01000057; EGL85104.1; -; Genomic_DNA.
DR   AlphaFoldDB; F5VX15; -.
DR   PATRIC; fig|1005704.3.peg.1754; -.
DR   eggNOG; COG3684; Bacteria.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000003695; Unassembled WGS sequence.
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   326 AA;  36238 MW;  79750B01AB349B3A CRC64;
     MALTEQKRAR LEKLSDENGI ISALAFDQRG ALKRLMAQYQ TEEPTVAQME ELKVLVADEL
     TKYASSMLLD PEYGLPATKA LDPNAGLLLA YEKTGYDTTS TKRLPDCLDV WSAKRIKEQG
     ADAVKFLLYY DVDSADELNQ QKQAYIERIG SECVAEDIPF FLEILAYDEK IADAGSAEYA
     KVKPHKVIGA MKVFSDPRFN IDVLKVEVPV NVKYVEGFGD GEIVHTREEA AAFFKAQDEA
     TNLPYIYLSA GVSAKLFQDT LVFAHESGAN FNGVLCGRAT WAGSVEAYIK DGEAAAREWL
     RTTGFENIDE LNKVLQTTAT SWKERV
//
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