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Database: UniProt
Entry: A0A0C1IRG3_9BACT
LinkDB: A0A0C1IRG3_9BACT
Original site: A0A0C1IRG3_9BACT 
ID   A0A0C1IRG3_9BACT        Unreviewed;       724 AA.
AC   A0A0C1IRG3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=sucrose-phosphate synthase {ECO:0000256|ARBA:ARBA00012536};
DE            EC=2.4.1.14 {ECO:0000256|ARBA:ARBA00012536};
GN   ORFNames=OI18_20050 {ECO:0000313|EMBL:KIC93039.1};
OS   Flavihumibacter solisilvae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavihumibacter.
OX   NCBI_TaxID=1349421 {ECO:0000313|EMBL:KIC93039.1, ECO:0000313|Proteomes:UP000031408};
RN   [1] {ECO:0000313|EMBL:KIC93039.1, ECO:0000313|Proteomes:UP000031408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3-3 {ECO:0000313|EMBL:KIC93039.1,
RC   ECO:0000313|Proteomes:UP000031408};
RA   Zhou G., Li M., Wang G.;
RT   "Genome sequence of Flavihumibacter solisilvae 3-3.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 6-phosphate + UDP-alpha-D-glucose = H(+) +
CC         sucrose 6(F)-phosphate + UDP; Xref=Rhea:RHEA:22172,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57634, ChEBI:CHEBI:57723,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00001481};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       {ECO:0000256|ARBA:ARBA00006530}.
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:KIC93039.1}.
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DR   EMBL; JSVC01000024; KIC93039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1IRG3; -.
DR   STRING; 1349421.OI18_20050; -.
DR   Proteomes; UP000031408; Unassembled WGS sequence.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR   GO; GO:0016157; F:sucrose synthase activity; IEA:InterPro.
DR   GO; GO:0046524; F:sucrose-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005985; P:sucrose metabolic process; IEA:InterPro.
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; IPR001296; Glyco_trans_1.
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   InterPro; IPR012821; Sucrose_P_synth_Pase-like_dom.
DR   InterPro; IPR000368; Sucrose_synth.
DR   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   NCBIfam; TIGR02471; sucr_syn_bact_C; 1.
DR   PANTHER; PTHR46039; SUCROSE-PHOSPHATE SYNTHASE 3-RELATED; 1.
DR   PANTHER; PTHR46039:SF5; SUCROSE-PHOSPHATE SYNTHASE 3-RELATED; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF05116; S6PP; 1.
DR   Pfam; PF00862; Sucrose_synth; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031408};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          8..208
FT                   /note="Sucrose synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00862"
FT   DOMAIN          257..433
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   DOMAIN          485..721
FT                   /note="Sucrose phosphatase-like"
FT                   /evidence="ECO:0000259|Pfam:PF05116"
SQ   SEQUENCE   724 AA;  82877 MW;  4BBB7C6E3C8BB904 CRC64;
     MKMKELYIQL FSPHGLIRYE NPEIGRDRDT GGQVKYVLEL LDHLSKHPQI RKVDLFTRRI
     SDKRVSSSYE SELELINEKA RIVRIPCGGH TYHPKESLWE YLDEFVDNTI RFIERQDDFP
     DAVHGHYADG NYLAGQISEV FGIPFIATGH SLGRNKQNIL LNQGLSQEKI NEKFCMERRI
     EVEENVLHDA DLVIVSTQHE IDQQYGLYKN REAGRFLVIP PGVNSELFYP FYRADMPGFK
     MTIEQEQALY RVNSDIERFL FNPAKPLILS IGRADKRKNF ETIIQSFGQD KELQAMANLA
     IFAGVRKDIT RMPEDEQDTL TNLLLLLDKY DLYGKMAIPK KNDPVLDVPE IYRVAARRKG
     AFVNATPGEN FGLTIVESAA CGLPVVASPT GGPKEIIENC DNGLLVDVEN PRAIADALKK
     IIADQAFWEK CSGNGVLATS QLYSWEAHCN KYVETIEALL SGRTTQTRKF SNRTAFGKKL
     MKAKQFIISD LDGTLVEGNQ TDGLIELKQW LLEHKDEVVF GIASGRNREI TKEAFEKYDL
     PKPDILICSA GSEIYYTDKF IPDKGWESHI DYKWKRKELE RELAKFPGIR LQEPAAQWPF
     KLSYYVNPDF AEDDFANLHK FLDDRRLRAK IMLTENKYLD LLPFRAGKGN AVRYLSSKWK
     VPLQHIITAG NSGNDIDMLT GRTKAIVVAN YSPEMEVLRN NKFIYFTRNN LSKGVLEGIN
     FHYS
//
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