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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
 
 
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