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Database: UniProt
Entry: A0A1Q3TQ35_9SPHI
LinkDB: A0A1Q3TQ35_9SPHI
Original site: A0A1Q3TQ35_9SPHI 
ID   A0A1Q3TQ35_9SPHI        Unreviewed;       754 AA.
AC   A0A1Q3TQ35;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Glucosylglycerol-phosphate synthase {ECO:0000313|EMBL:OJW04454.1};
GN   ORFNames=BGO52_18145 {ECO:0000313|EMBL:OJW04454.1};
OS   Sphingobacteriales bacterium 44-61.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895838 {ECO:0000313|EMBL:OJW04454.1, ECO:0000313|Proteomes:UP000186208};
RN   [1] {ECO:0000313|EMBL:OJW04454.1, ECO:0000313|Proteomes:UP000186208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44-61 {ECO:0000313|EMBL:OJW04454.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC       {ECO:0000256|ARBA:ARBA00008799}.
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:OJW04454.1}.
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DR   EMBL; MKTW01000001; OJW04454.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3TQ35; -.
DR   STRING; 1895838.BGO52_18145; -.
DR   Proteomes; UP000186208; Unassembled WGS sequence.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR   GO; GO:0051473; P:glucosylglycerol biosynthetic process; IEA:InterPro.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR   CDD; cd03788; GT20_TPS; 1.
DR   Gene3D; 3.90.1070.10; -; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR012764; Gluc_glyc_Psyn.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006380; SPP-like_dom.
DR   NCBIfam; TIGR02398; gluc_glyc_Psyn; 1.
DR   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   PANTHER; PTHR10788:SF106; BCDNA.GH08860; 1.
DR   PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   Pfam; PF05116; S6PP; 1.
DR   SFLD; SFLDG01141; C2.B.1:_Sucrose_Phosphatase_Li; 1.
DR   SFLD; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
FT   DOMAIN          2..231
FT                   /note="Sucrose phosphatase-like"
FT                   /evidence="ECO:0000259|Pfam:PF05116"
SQ   SEQUENCE   754 AA;  85152 MW;  5F4F82FD18533A8E CRC64;
     MLLATDLDGT FLGGTSLHKQ QLYRLIRQNM DARLVFVTGR GLESVMPLLN DPIIPNPDYI
     ICDVGATIVN GHTLEPVETL QSEIEKNWPG SLKVMETLAG SDDIQHQEVP QQRRSSFYVQ
     SEETVAKVRE LVATLNCDVV HSAGKFLDVL PHGVNKGTSL KKLVNYLRYN PEDVLVAGDT
     LNDLAMYQCS FKGVVVGRSE KKLIEATSGI EGVYHANAAG AGGILEALHH FPGLVSDLEL
     EEVRPMENAA ANSSQLIMMY HRFPYEKKEI NGHVQRVAPK SPNGILPTLQ GFFAGGRSGL
     WIAWEEVEQP GEALRNIYID KTTYPNLMAA RVGLTKEEVN IFYKSFSKEA FWPMIFSFID
     KVHFDHNHWD HFQAINHRFA EKAAEQADQG AIVWIHDYNL WLVPGYLRQL RPDLTIAFFH
     HTAFPAANTF NILPWRREII GSLLQCDFIG FHIPRYVENF VDVASSLFPI TTYPKVNCAP
     RFLTYSSAIG VSSMTPAIET GERTVSLGAV PVGINTEYIN QLFQDGLMQE KIKTLKQQLN
     GKKMILSAER LDYVKGPLEK ILAFEHFLEE YPEFHGKVEL VNICPPAAEG MKIYDDIKLQ
     LEQAVGRING KYANIDWTPI RIFFRSFPFE DILVYYGAAD IAWITPLRDG LNLVAKEFIA
     VQGESQQDKG VLILSEFAGS SVELSYALLT NPYDLRSLKE TLLQALLMRP EERNMRMERL
     YEQIKHYDIE YWANDFIRKA SASVTPELEA VVSI
//
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