ID F5SUP6_9GAMM Unreviewed; 716 AA.
AC F5SUP6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=sucrose-phosphate synthase {ECO:0000256|ARBA:ARBA00012536};
DE EC=2.4.1.14 {ECO:0000256|ARBA:ARBA00012536};
GN ORFNames=MAMP_02538 {ECO:0000313|EMBL:EGL55544.1};
OS Methylophaga aminisulfidivorans MP.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL55544.1, ECO:0000313|Proteomes:UP000003544};
RN [1] {ECO:0000313|EMBL:EGL55544.1, ECO:0000313|Proteomes:UP000003544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX PubMed=21685284; DOI=10.1128/JB.05403-11;
RA Han G.H., Kim W., Chun J., Kim S.W.;
RT "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL J. Bacteriol. 193:4265-4265(2011).
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:EGL55544.1}.
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DR EMBL; AFIG01000001; EGL55544.1; -; Genomic_DNA.
DR RefSeq; WP_007145430.1; NZ_AFIG01000001.1.
DR AlphaFoldDB; F5SUP6; -.
DR STRING; 1026882.MAMP_02538; -.
DR eggNOG; COG0438; Bacteria.
DR eggNOG; COG0561; Bacteria.
DR OrthoDB; 7847955at2; -.
DR Proteomes; UP000003544; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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 CDD; cd03800; GT4_sucrose_synthase; 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; 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 InterPro; IPR012822; SucroseP_synth_GlycoTrfase_dom.
DR NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR NCBIfam; TIGR02472; sucr_P_syn_N; 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:UP000003544};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGL55544.1}.
FT DOMAIN 10..210
FT /note="Sucrose synthase"
FT /evidence="ECO:0000259|Pfam:PF00862"
FT DOMAIN 253..424
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT DOMAIN 470..706
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
SQ SEQUENCE 716 AA; 80890 MW; 13C76FEF9695DC8C CRC64;
MGDTVEQMYI ALISVHGLIR ADNLELGRDA DTGGQTLYVL ELAQALSELP NVSQVDLVTR
RIIDSHVDAD YAEPIEVVNE KFRIVRIDAG PEEYIYKEQL WEHLDGFADN LADFFRKQDH
IPDLIHSHYA DAGLVGSHVA NLLGIPLVHT GHSLGRVKRR RLLASGLTTE QIESLYNMTR
RIEAEEITLA TAERVITSTH QEIEEQYEIY DHYQPDQMRV IPPGTNIKQF KPPEGNELET
ELFGKLTHQL VEPNKPVILA LSRPDKRKNI AVLIEAYGES ERLQQLANLV IIAGNRDDID
DLEAGAQEVF HELLVAIDRY DLYGKVAMPK HHKREQVPLM YRIAAASGGV FVNPALTEPF
GLTLIEAAAS GVPIIATEDG GPRDIIGNCH NGILIDPLET STITDALLKL LTDNALWNDY
SSNGLEGVAK CYSWQAHAKR YIELVTPLAQ RAELLQRQPL ERTSHVYAEQ AIFTDLDLNL
IGDDVSLHKL INLIRENRKT TKFAIATGRR LDVALRMMKK HQIPEPDILI TSSGTEIYYA
PKLTPDTSWA QHIDYHWTPH KVRQLLDDYP GLEKQPKAEQ SRFKLSYYID PEQADIEEIK
RLLHQEEQSV HVQLAFGQYL DILPIRASKG MALRYVADHW QIPLEHIFVA GGSGADEDMM
RGNTLAAVVA NRHNEELSQL IDTDRIYFAD KPFAAGILES LEHYQFFHQA KTKKTS
//
