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
//