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Database: UniProt
Entry: B9I867_POPTR
LinkDB: B9I867_POPTR
Original site: B9I867_POPTR 
ID   B9I867_POPTR            Unreviewed;      1020 AA.
AC   B9I867;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 2.
DT   27-MAR-2024, entry version 93.
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=POPTR_013G095500 {ECO:0000313|EMBL:PNT07587.1};
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT07587.1, ECO:0000313|Proteomes:UP000006729};
RN   [1] {ECO:0000313|EMBL:PNT07587.1, ECO:0000313|Proteomes:UP000006729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX   PubMed=16973872; DOI=10.1126/science.1128691;
RA   Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA   Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA   Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA   Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA   Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA   Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA   Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA   Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA   Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA   Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA   Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA   Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA   Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA   Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA   Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA   Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA   Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA   Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA   Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA   Rokhsar D.;
RT   "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL   Science 313:1596-1604(2006).
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|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; CM009302; PNT07587.1; -; Genomic_DNA.
DR   RefSeq; XP_002319320.2; XM_002319284.2.
DR   AlphaFoldDB; B9I867; -.
DR   STRING; 3694.B9I867; -.
DR   GeneID; 7477753; -.
DR   KEGG; pop:7477753; -.
DR   eggNOG; KOG0853; Eukaryota.
DR   HOGENOM; CLU_009583_24_0_1; -.
DR   InParanoid; B9I867; -.
DR   OMA; YEAHVEY; -.
DR   OrthoDB; 1206157at2759; -.
DR   UniPathway; UPA00371; UER00545.
DR   Proteomes; UP000006729; Chromosome 13.
DR   ExpressionAtlas; B9I867; baseline and differential.
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; cd03800; GT4_sucrose_synthase; 1.
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:SF1; SUCROSE-PHOSPHATE SYNTHASE 4; 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:UP000006729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368006}.
FT   DOMAIN          166..428
FT                   /note="Sucrose synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00862"
FT   DOMAIN          470..643
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   DOMAIN          781..967
FT                   /note="Sucrose phosphatase-like"
FT                   /evidence="ECO:0000259|Pfam:PF05116"
FT   REGION          116..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1020 AA;  115481 MW;  4D53ED8BD958C298 CRC64;
     MARNEWINGY LEAILDVGSG VMKKRSDGRL KIAKFQQVKE DKLFSPIKYF VEEVINSFDE
     SDLHRTWVKM IATRNTRERS NRLENMCWRI WHLARKKKQI AWDDAQRLAK RRLEREQGRN
     DAADDLSELS EGEKEKGEAN LSESVRDIAR INSDMKLWSD DDKPRQLYIV LISMHGLVRG
     ENMELGRDSD TGGQVKYVVE LARALANTKG VYRVDLLTRQ ITSPEVDFSY GEPIEMLSCP
     SDDSGSCGAY IIRIPCGPQD RYIPKESLWP WIPEFVDGAL NHIVNMARAL GEQVNGGKPT
     WPYVIHGHYA DAGEVAALLS GALNVPMVLT GHSLGRNKFE QLLKQGRHSK EHINATYKIM
     RRIEAEELGL DAAEMVVTST RQEIEEQWGL YDGFDIKVER KLRVRRRRGV SCLGRYMPRM
     VVIPPGMDFS YVTADDSLEG DLKSLIDSDR NQNKRSLPPI WSEIMRFFTN PHKPTILALS
     RPDPKKNVTT LLQAFGECQP LRELANLTLI LGNRDDIGEM SDSSSSVLTN VLKLIDKYDL
     YGQVAYPKHH KQSDVPDIYR LAAKTKGVFI NPALVEPFGL TLIEAAAYGL PVVATKNGGP
     VDISKVLHNG LLVDPHDQKA IADALLKLVA DKNLWTECRK NGLKNIHSFS WPEHCRNYLS
     HIEQCRNRHP TTRLEITPLP EEPMSESLKD MEDLSLRFSI EGDYKLNGEL DATNKQKKLI
     EAITQMAPSN GKASVTYTPG RRQMLFVIAT DCYSFNGQST ETFQEIIKNV MKAGGQSLGM
     DRIGFVLATS SSLQEIMEAL RCCEVKIEDF DAIICNSGGN MYYPWRDMVV DVDYEAHVDY
     RWPGENVRSM VMRLARAEDG AEDDIKEYIK ASSSRCFSYS IKPGVKTRKV YELRQRLRMR
     GLRCNIVYTH AASRLNVTPI FASRTQALRY LSVRWGIDLS KMVVFVGGRG DTDYEDLLAG
     LHKTIIIRGL VEYGSEKLLH SAESFKREDV VPQESSNISF VEEKYEAADI SAALVAMGIK
//
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