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Database: UniProt
Entry: A0A1H6RL21_9LACT
LinkDB: A0A1H6RL21_9LACT
Original site: A0A1H6RL21_9LACT 
ID   A0A1H6RL21_9LACT        Unreviewed;       331 AA.
AC   A0A1H6RL21;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN04488113_10381 {ECO:0000313|EMBL:SEI56508.1};
OS   Alkalibacterium gilvum.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alkalibacterium.
OX   NCBI_TaxID=1130080 {ECO:0000313|EMBL:SEI56508.1, ECO:0000313|Proteomes:UP000198564};
RN   [1] {ECO:0000313|Proteomes:UP000198564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25751 {ECO:0000313|Proteomes:UP000198564};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNYW01000003; SEI56508.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6RL21; -.
DR   STRING; 1130080.SAMN04488113_10381; -.
DR   OrthoDB; 106309at2; -.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000198564; 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   331 AA;  37312 MW;  5C084791FD040078 CRC64;
     MKTISKNKYE AMERLSTKEG VISALAIDQR GSLKKMIAEG SKEKIGDEGI IEFKKLISKV
     LTPYSSSILL DPEYGIPATK ERDSESGLLL AYEKTGYDAT EPGRLPDLLE EWSVKRLKEA
     GVDAVKFLLY YDVDEDEKIN EFKHVYMERV GSECIGEDIP FFLEIVTYDS KIDDAKGKDY
     AKVKPHKVIE AMKEFSKPRY NVDVLKVEVP VHMQYVEGFA EAGEEVYSKE EAQGYYKEQS
     EATDLPFIFL SAGVSAQMFQ ETLKFAHEAK STFNGVLCGR ATWKNSVLPY ASEGKQAGED
     WLSDQGVRNI TELNDVVDVT ALSWKEKIKQ A
//
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