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Database: UniProt
Entry: A9C135_DELAS
LinkDB: A9C135_DELAS
Original site: A9C135_DELAS 
ID   A9C135_DELAS            Unreviewed;       514 AA.
AC   A9C135;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Alpha,alpha-trehalose-phosphate synthase (UDP-forming) {ECO:0000313|EMBL:ABX38498.1};
DE            EC=2.4.1.15 {ECO:0000313|EMBL:ABX38498.1};
GN   OrderedLocusNames=Daci_5870 {ECO:0000313|EMBL:ABX38498.1};
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX38498.1, ECO:0000313|Proteomes:UP000000784};
RN   [1] {ECO:0000313|EMBL:ABX38498.1, ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX   PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA   Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT   "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT   defined pairs of heterotrophic bacteria.";
RL   Appl. Environ. Microbiol. 70:4053-4063(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC       {ECO:0000256|ARBA:ARBA00008799}.
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DR   EMBL; CP000884; ABX38498.1; -; Genomic_DNA.
DR   RefSeq; WP_012207667.1; NC_010002.1.
DR   AlphaFoldDB; A9C135; -.
DR   STRING; 398578.Daci_5870; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   GeneID; 24116563; -.
DR   KEGG; dac:Daci_5870; -.
DR   eggNOG; COG0380; Bacteria.
DR   HOGENOM; CLU_002351_7_1_4; -.
DR   Proteomes; UP000000784; Chromosome.
DR   GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR   CDD; cd03788; GT20_TPS; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   PANTHER; PTHR10788:SF106; BCDNA.GH08860; 1.
DR   PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000313|EMBL:ABX38498.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000784};
KW   Transferase {ECO:0000313|EMBL:ABX38498.1}.
FT   REGION          460..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  57361 MW;  22EB1D77E9792CB2 CRC64;
     MSRLVVISNR VADPAKAAAG GLAVAMGDAL RQTGGLWFGW SGTVTDGHAA APAGHVHRTQ
     AGKVTLATVD LDRADHDSYY AGYSNGVLWP VFHGRLDLAN FDTGLAAGYR RVNQLLARRL
     LPLLAEDDIL WVHDYHLIPL AAELRALGCR QRIGFFLHIP LPPPTLLAAI PEHAWLMRCL
     FAYDLMGLQT RQDVQHFERY VCEEAGGQTL GDGAFRAHGQ RMVCRDFPIG IDVDGFMALA
     QGGASRDMYE RMKHEYAQRR LLLGIDRLDY SKGLPQRLRA FRELLARHPE QRRRATLIQI
     GSPTREGLDA YADIRRELES LCGAINGDYG ELDWMPVRYI HQTLPRDSIP GLCRAAAVGL
     VTPLRDGMNL VAKEYVAAQD PADPGVLVLS RFAGAAEQLH EALLVNPYDV HGTAAVVQQA
     LHMPLHERRQ RHQRLLQRVC EQDVHWWRKA FLSALKETRP QERRDRDWSK EREAGFGIPV
     PSMRQERPPL GLELPACPAD ALALDASRSV VSDR
//
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