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
//