SUS6_ARATH
ID SUS6_ARATH Reviewed; 942 AA.
AC Q9FX32;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Sucrose synthase 6;
DE Short=AtSUS6;
DE EC=2.4.1.13;
DE AltName: Full=Sucrose-UDP glucosyltransferase 6;
GN Name=SUS6; OrderedLocusNames=At1g73370; ORFNames=T9L24.42;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND TISSUE SPECIFICITY.
RX PubMed=14739263; DOI=10.1093/jxb/erh047;
RA Baud S., Vaultier M.N., Rochat C.;
RT "Structure and expression profile of the sucrose synthase multigene family
RT in Arabidopsis.";
RL J. Exp. Bot. 55:397-409(2004).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17257168; DOI=10.1111/j.1365-313x.2006.03011.x;
RA Bieniawska Z., Paul Barratt D.H., Garlick A.P., Thole V., Kruger N.J.,
RA Martin C., Zrenner R., Smith A.M.;
RT "Analysis of the sucrose synthase gene family in Arabidopsis.";
RL Plant J. 49:810-828(2007).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=18635527; DOI=10.1093/jxb/ern180;
RA Fallahi H., Scofield G.N., Badger M.R., Chow W.S., Furbank R.T., Ruan Y.L.;
RT "Localization of sucrose synthase in developing seed and siliques of
RT Arabidopsis thaliana reveals diverse roles for SUS during development.";
RL J. Exp. Bot. 59:3283-3295(2008).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=19470642; DOI=10.1073/pnas.0900689106;
RA Barratt D.H., Derbyshire P., Findlay K., Pike M., Wellner N., Lunn J.,
RA Feil R., Simpson C., Maule A.J., Smith A.M.;
RT "Normal growth of Arabidopsis requires cytosolic invertase but not sucrose
RT synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:13124-13129(2009).
CC -!- FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and
CC fructose for various metabolic pathways. Functions in callose synthesis
CC at the site of phloem sieve elements. {ECO:0000269|PubMed:19470642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an NDP-alpha-D-glucose + D-fructose = a ribonucleoside 5'-
CC diphosphate + H(+) + sucrose; Xref=Rhea:RHEA:16241,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17992, ChEBI:CHEBI:37721,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:76533; EC=2.4.1.13;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.44 mM for D-fructose (synthetic reaction)
CC {ECO:0000269|PubMed:17257168};
CC KM=0.06 mM for UDP-glucose (synthetic reaction)
CC {ECO:0000269|PubMed:17257168};
CC KM=31.06 mM for sucrose (degradative reaction)
CC {ECO:0000269|PubMed:17257168};
CC KM=0.26 mM for UDP (degradative reaction)
CC {ECO:0000269|PubMed:17257168};
CC Vmax=3.27 umol/min/mg enzyme for synthetic reaction
CC {ECO:0000269|PubMed:17257168};
CC Vmax=1.43 umol/min/mg enzyme for degradative reaction
CC {ECO:0000269|PubMed:17257168};
CC pH dependence:
CC Optimum pH is 6.0-7.0 for degradative reaction (PubMed:22184213,
CC PubMed:17257168). Optimum pH is 7.0 for synthetic reaction
CC (PubMed:22184213). Optimum pH is 9.0-9.5 for synthetic reaction
CC (PubMed:17257168). {ECO:0000269|PubMed:17257168};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:19470642}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FX32-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Detected in the whole plant but more precisely
CC confined to the vasculature in cotyledons, leaves, petals, anthers and
CC roots. {ECO:0000269|PubMed:14739263, ECO:0000269|PubMed:17257168,
CC ECO:0000269|PubMed:18635527, ECO:0000269|PubMed:19470642}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17257168}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. Plant sucrose
CC synthase subfamily. {ECO:0000305}.
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DR EMBL; AC012396; AAG30975.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35450.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59229.1; -; Genomic_DNA.
DR PIR; C96760; C96760.
DR RefSeq; NP_001319374.1; NM_001334591.1. [Q9FX32-1]
DR RefSeq; NP_177480.1; NM_105997.2. [Q9FX32-1]
DR AlphaFoldDB; Q9FX32; -.
DR SMR; Q9FX32; -.
DR STRING; 3702.AT1G73370.1; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; Q9FX32; -.
DR PaxDb; Q9FX32; -.
DR PRIDE; Q9FX32; -.
DR ProteomicsDB; 228435; -. [Q9FX32-1]
DR EnsemblPlants; AT1G73370.1; AT1G73370.1; AT1G73370. [Q9FX32-1]
DR EnsemblPlants; AT1G73370.3; AT1G73370.3; AT1G73370. [Q9FX32-1]
DR GeneID; 843672; -.
DR Gramene; AT1G73370.1; AT1G73370.1; AT1G73370. [Q9FX32-1]
DR Gramene; AT1G73370.3; AT1G73370.3; AT1G73370. [Q9FX32-1]
DR KEGG; ath:AT1G73370; -.
DR Araport; AT1G73370; -.
DR TAIR; locus:2206865; AT1G73370.
DR eggNOG; KOG0853; Eukaryota.
DR InParanoid; Q9FX32; -.
DR PhylomeDB; Q9FX32; -.
DR BioCyc; MetaCyc:AT1G73370-MON; -.
DR BRENDA; 2.4.1.13; 399.
DR PRO; PR:Q9FX32; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FX32; baseline and differential.
DR Genevisible; Q9FX32; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016157; F:sucrose synthase activity; IDA:TAIR.
DR GO; GO:0080165; P:callose deposition in phloem sieve plate; IMP:TAIR.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:InterPro.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR000368; Sucrose_synth.
DR InterPro; IPR012820; Sucrose_synthase_pln/cyn.
DR PANTHER; PTHR45839; PTHR45839; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF00862; Sucrose_synth; 1.
DR TIGRFAMs; TIGR02470; sucr_synth; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell wall; Glycosyltransferase; Reference proteome;
KW Secreted; Transferase.
FT CHAIN 1..942
FT /note="Sucrose synthase 6"
FT /id="PRO_0000418805"
FT REGION 281..759
FT /note="GT-B glycosyltransferase"
FT /evidence="ECO:0000250"
FT REGION 830..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 942 AA; 106876 MW; 0AA4A92EC48815EA CRC64;
MSSSSQAMLQ KSDSIAEKMP DALKQSRYHM KRCFASFVGG GKKLMKREHL MNEIEKCIED
SRERSKILEG LFGYILTCTQ EAAVVPPFVA LAARPNPGFW EYVKVNSGDL TVDEITATDY
LKLKESVFDE SWSKDENALE IDFGAIDFTS PRLSLSSSIG KGADYISKFI SSKLGGKSDK
LEPLLNYLLR LNHHGENLMI NDDLNTVAKL QKSLMLAVIV VSTYSKHTPY ETFAQRLKEM
GFEKGWGDTA ERVKETMIIL SEVLEAPDNG KLDLLFSRLP TVFNVVIFSV HGYFGQQDVL
GLPDTGGQVV YILDQVRALE EELLIRINQQ GLGFKPQILV VTRLIPEARG TKCDQELEAI
EGTKHSHILR VPFVTNKGVL RQWVSRFDIY PYLERFTQDA TSKILQRLDC KPDLIIGNYT
DGNLVASLMA TKLGVTQGTI AHALEKTKYE DSDAKWKELD PKYHFSCQFT ADLIAMNVTD
FIITSTYQEI AGSKDRPGQY ESHTAFTMPG LCRVVSGIDV FDPKFNIAAP GADQSVYFPY
TEKDKRFTKF HPSIQELLYN EKDNAEHMGY LADREKPIIF SMARLDTVKN ITGLVEWYGK
DKRLREMANL VVVAGFFDMS KSNDREEKAE IKKMHDLIEK YKLKGKFRWI AAQTDRYRNS
ELYRCIADTK GVFVQPALYE AFGLTVIEAM NCGLPTFATN QGGPAEIIVD GVSGFHIDPN
NGDESVTKIG DFFSKCRSDG LYWDNISKGG LKRIYECYTW KIYAEKLLKM GSLYGFWRQV
NEDQKKAKKR YIEMLYNLQF KQLTKKVTIP EDKPLPLRLA SLRNLLPKKT TNLGAGSKQK
EVTETEKTKQ KSKDGQEQHD VKVGEREVRE GLLAADASER VKKVLESSEE KQKLEKMKIA
YGQQHSQGAS PVRNLFWSVV VCLYICYILK QRFFGANSAQ EY
