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Database: UniProt
Entry: A0A062X452_9LACO
LinkDB: A0A062X452_9LACO
Original site: A0A062X452_9LACO 
ID   A0A062X452_9LACO        Unreviewed;       327 AA.
AC   A0A062X452;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   ORFNames=Lani381_1386 {ECO:0000313|EMBL:KDA45538.1};
OS   Ligilactobacillus animalis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1605 {ECO:0000313|EMBL:KDA45538.1, ECO:0000313|Proteomes:UP000027129};
RN   [1] {ECO:0000313|EMBL:KDA45538.1, ECO:0000313|Proteomes:UP000027129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=381-IL-28 {ECO:0000313|EMBL:KDA45538.1,
RC   ECO:0000313|Proteomes:UP000027129};
RA   Sturino J.M., Rajendran M., Altermann E.;
RT   "Draft Genome Sequence of Lactobacillus animalis 381-IL-28.";
RL   Submitted (APR-2014) 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:KDA45538.1}.
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DR   EMBL; JMHU01000019; KDA45538.1; -; Genomic_DNA.
DR   RefSeq; WP_035448755.1; NZ_POVP01000008.1.
DR   AlphaFoldDB; A0A062X452; -.
DR   PATRIC; fig|1605.9.peg.1359; -.
DR   eggNOG; COG3684; Bacteria.
DR   OrthoDB; 106309at2; -.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000027129; 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   327 AA;  35746 MW;  653DB7F6A2353EEB CRC64;
     MIGKITALQR LSNSDGIIAA LAIDQRGSLK KMLAKKADHP VTSSDLSEFK KVISQKMTAY
     SSAILLDPEY GLPAALARDS NCGLLLAYEK TGYDVSEPGR MPDLLPDWSA KRLKEAGADA
     VKFMVYYDVD EPMAINEKKQ AFIERIGSEC VAEDIPFFLE LMSYDANIED TKSKEYAAVK
     PHKVIEMMRE FAKPRYNVDV LKVEVPVNMA YVAGFAKDED AVYTKEQAAA YFAEQTKAAA
     GVPFIFLSAG VSAQMFQDTL YFAHEAGSKF NGVLCGRATW KDSVVPFAQD GAGAASLWCE
     TQGKANIEAL NTVLKETATP LASKNLI
//
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