ID A0A3B6RNZ5_WHEAT Unreviewed; 972 AA.
AC A0A3B6RNZ5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Sucrose-phosphate synthase {ECO:0000256|ARBA:ARBA00012536, ECO:0000256|RuleBase:RU368006};
DE EC=2.4.1.14 {ECO:0000256|ARBA:ARBA00012536, ECO:0000256|RuleBase:RU368006};
GN ORFNames=CFC21_100344 {ECO:0000313|EMBL:KAF7098618.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS7A02G518200.1};
RN [1] {ECO:0000313|EMBL:KAF7098618.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7098618.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS7A02G518200.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS7A02G518200.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS7A02G518200.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7098618.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7098618.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in photosynthetic sucrose synthesis by
CC catalyzing the rate-limiting step of sucrose biosynthesis from UDP-
CC glucose and fructose- 6-phosphate. Involved in the regulation of carbon
CC partitioning in the leaves of plants. May regulate the synthesis of
CC sucrose and therefore play a major role as a limiting factor in the
CC export of photoassimilates out of the leaf. Plays a role for sucrose
CC availability that is essential for plant growth and fiber elongation.
CC {ECO:0000256|ARBA:ARBA00024883, ECO:0000256|RuleBase:RU368006}.
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 ECO:0000256|RuleBase:RU368006};
CC -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-
CC fructose 6-phosphate and UDP-alpha-D-glucose: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005027, ECO:0000256|RuleBase:RU368006}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|ARBA:ARBA00011774,
CC ECO:0000256|RuleBase:RU368006}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC {ECO:0000256|ARBA:ARBA00006530, ECO:0000256|RuleBase:RU368006}.
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DR EMBL; CM022229; KAF7098618.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6RNZ5; -.
DR SMR; A0A3B6RNZ5; -.
DR STRING; 4565.A0A3B6RNZ5; -.
DR EnsemblPlants; TraesCS7A02G518200.1; TraesCS7A02G518200.1; TraesCS7A02G518200.
DR Gramene; TraesCAD_scaffold_099386_01G000100.1; TraesCAD_scaffold_099386_01G000100.1; TraesCAD_scaffold_099386_01G000100.
DR Gramene; TraesCS7A02G518200.1; TraesCS7A02G518200.1; TraesCS7A02G518200.
DR Gramene; TraesCS7A03G1258800.1; TraesCS7A03G1258800.1.CDS; TraesCS7A03G1258800.
DR Gramene; TraesKAR7A01G0450800.1; cds.TraesKAR7A01G0450800.1; TraesKAR7A01G0450800.
DR Gramene; TraesPAR_scaffold_129672_01G000100.1; TraesPAR_scaffold_129672_01G000100.1; TraesPAR_scaffold_129672_01G000100.
DR Gramene; TraesWEE_scaffold_135207_01G000100.1; TraesWEE_scaffold_135207_01G000100.1; TraesWEE_scaffold_135207_01G000100.
DR OrthoDB; 350804at2759; -.
DR UniPathway; UPA00371; UER00545.
DR Proteomes; UP000019116; Chromosome 7A.
DR Proteomes; UP000815260; Chromosome 7A.
DR GO; GO:0016157; F:sucrose synthase activity; IEA:InterPro.
DR GO; GO:0046524; F:sucrose-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd16419; HAD_SPS; 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; IPR023214; HAD_sf.
DR InterPro; IPR006380; SPP-like_dom.
DR InterPro; IPR035659; SPS_C.
DR InterPro; IPR012819; SPS_pln.
DR InterPro; IPR000368; Sucrose_synth.
DR NCBIfam; TIGR02468; sucrsPsyn_pln; 1.
DR PANTHER; PTHR46039; SUCROSE-PHOSPHATE SYNTHASE 3-RELATED; 1.
DR PANTHER; PTHR46039:SF4; 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; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU368006};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368006}.
FT DOMAIN 166..432
FT /note="Sucrose synthase"
FT /evidence="ECO:0000259|Pfam:PF00862"
FT DOMAIN 468..641
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT DOMAIN 803..912
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
SQ SEQUENCE 972 AA; 108656 MW; BFF8FBB314BB57DC CRC64;
MYGNDNWINS YLDAILDAGK GAGSGSGGGG GGGAGGDRPS LLLRERGHFS PARYFVEEVI
TGYDETDLYK TWSRANAMRS PQERNTRLEN MTWRIWNLAR KKKEVEDAKR LKRRLETEKP
RTDATAEMSE DLFEGEKGED AGDASVAYGD SSAGNTPRIS AVDKLYIVLI SLHGLVRGEN
LELGRDSDTS GQVKYVVELA KALSSCPGVY RVDLLTRQIL APNYDRGYGE PSETLVPTSF
KNLKQERGEN SGAYITRIPF GPKDKYLAKE HLWPYVQEFV DGALSHIVHM SKIIGEEIGC
GHPMWPAVIH GHYASAGVAA ALISGALNVH MVFTGHFLGK DKLEGLLKQG RQTREEINMT
YKIMRRIEAE ELSLDASEIV IASTRQEIEE QWNLYDGFEV MLARKLRARV KRGANCYGRY
MPRMVIIPPG VEFGHMIHEF DMEGEEDSHS PASEDPPIWS EIMRFFTNPR KPLILAVARP
YPEKNITTLV KAFGECRPLR ELANLTLIMG NREAISKMSN MSAAVLTSVL TLIDEYDLYG
QVAYPKHHKH SEVLDIYRLA ARTKGAFVNV AYFEQFGVTL IEAAMHGLPV IATKNGAPVE
IHQVLDNGLL VDPHDQHAIA DALYKLLSDK QLWSRCRENG LKNIHRFSWP EHCKNYLSRI
LTLSPRYPAF PGNEDQIKAP IKERKCIIVI AVDSASKKDL VCIIKNSIEA TRKETLSGST
GFVLSTSLTM SEIHSLLISA GMAPTDFDAF ICNSGSDLFY PSRAGDSPST SRVTFALDRT
YQSHIEYRWG GEGLRKYLVK WASSIVERRG RTEKQVIFED AEHSSTCCFA FRVVNPNYLP
PLKELQKLMR IQSLRCHALY NHSATRLSVI PIHASRSQAL RYLSVRWGIE LRNVVILVGE
SGDSDYEELF GGLHKTIVLK GEFNTPANRI HTVRRYPLQD VIALDCSNII GVEGCSADDL
TPTLKTLGIP TK
//
