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Database: UniProt
Entry: A0A0R2FQ75_9LACO
LinkDB: A0A0R2FQ75_9LACO
Original site: A0A0R2FQ75_9LACO 
ID   A0A0R2FQ75_9LACO        Unreviewed;       350 AA.
AC   A0A0R2FQ75;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=IV38_GL000142 {ECO:0000313|EMBL:KRN29260.1}, IV40_GL000583
GN   {ECO:0000313|EMBL:KRN29782.1};
OS   Lactobacillus selangorensis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=81857 {ECO:0000313|EMBL:KRN29782.1, ECO:0000313|Proteomes:UP000051645};
RN   [1] {ECO:0000313|Proteomes:UP000051645, ECO:0000313|Proteomes:UP000051751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-66 {ECO:0000313|EMBL:KRN29260.1,
RC   ECO:0000313|Proteomes:UP000051751}, and DSM 13344
RC   {ECO:0000313|EMBL:KRN29782.1, ECO:0000313|Proteomes:UP000051645};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRN29782.1}.
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DR   EMBL; JQAT01000001; KRN29260.1; -; Genomic_DNA.
DR   EMBL; JQAZ01000012; KRN29782.1; -; Genomic_DNA.
DR   RefSeq; WP_057771253.1; NZ_JQAZ01000012.1.
DR   AlphaFoldDB; A0A0R2FQ75; -.
DR   STRING; 81857.IV38_GL000142; -.
DR   PATRIC; fig|81857.3.peg.147; -.
DR   OrthoDB; 106309at2; -.
DR   UniPathway; UPA00704; UER00716.
DR   Proteomes; UP000051645; Unassembled WGS sequence.
DR   Proteomes; UP000051751; 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   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:UP000051645}.
SQ   SEQUENCE   350 AA;  39064 MW;  FBEF5795DFA11BCC CRC64;
     MAKKRISRGK FDKLNQLSND KGVIAALAID QRGSMKKIMK AADEKAGKEY NIEQVYEFKE
     LVSQELTKYV SAILTDEELG FKAMKAKDPS AGLILSYEKT GYDVNTKGRY PELLQNESMQ
     RLLAKGADAA KVLVYYNPND PDEINDIKHA FLERIGDEGL AADIPLFVEI VTYDDSIPDV
     KSAEYAKEKP ELVINAMKDF NKPNYHIDVI KAEVPVNFAM VEGYAKDGVK PVYSQDEAAK
     IFASVNDVVD RPFIYLSAGV PAEEFRDELI FAGKSGNHFS GILGGRATWL DGVQVYADKG
     RDGLINWLDT QGKENVEELN NILDKYATPW EDVYGGADNI EVFDKQVMTD
//
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