ID E8X1Z5_GRATM Unreviewed; 335 AA.
AC E8X1Z5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=tagatose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00012905};
DE EC=4.1.2.40 {ECO:0000256|ARBA:ARBA00012905};
GN OrderedLocusNames=AciX9_2112 {ECO:0000313|EMBL:ADW69156.1};
OS Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343};
RN [1] {ECO:0000313|Proteomes:UP000000343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M.,
RA Haggblom M.M., Woyke T.;
RT "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9.";
RL Submitted (JAN-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};
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}.
CC -!- SIMILARITY: Belongs to the aldolase LacD family.
CC {ECO:0000256|ARBA:ARBA00008679}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002480; ADW69156.1; -; Genomic_DNA.
DR RefSeq; WP_013580472.1; NC_015064.1.
DR AlphaFoldDB; E8X1Z5; -.
DR STRING; 1198114.AciX9_2112; -.
DR PaxDb; 1198114-AciX9_2112; -.
DR KEGG; acm:AciX9_2112; -.
DR eggNOG; COG3684; Bacteria.
DR HOGENOM; CLU_058971_0_1_0; -.
DR OrthoDB; 106309at2; -.
DR UniPathway; UPA00704; UER00716.
DR Proteomes; UP000000343; Chromosome.
DR GO; GO:0009024; F:tagatose-6-phosphate kinase activity; IEA:InterPro.
DR GO; GO:0009025; F:tagatose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
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:InterPro.
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};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ADW69156.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000343}.
SQ SEQUENCE 335 AA; 36398 MW; 421394C4E45D87D1 CRC64;
MKLTPGKLAG LKAVSDARGV IAAAAMDQRG SLQKSLAKER GGIIDSAALG EFKTLVTEVL
TRHASAILLD PEFGLEASKN RNSAGLLLAY EKTGYDSATP GRLPDLLDVW SVRRLKEAGA
DCVKILLYYS PFEKTAINDL KHAWIERIGD ECIAHDIPFF LEFVGYDAEG GDEKSLAYAI
KKPLIVSGSM AEFGKERYNV DVLKVEVPVE MSYVEGTKAF KGEKAYTRAE ALQHFRDAET
MTHKPFIYLS AGVSNPVFIE TLALAAESGT KFNGVLCGRA TWKDGIVIYA KQGAAAFKEW
LETTGVENIS NVNEALKAAT PWYTKFGANS LAELG
//
