SUS5_ARATH
ID SUS5_ARATH Reviewed; 836 AA.
AC F4K5W8; Q9FHU4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Sucrose synthase 5;
DE Short=AtSUS5;
DE EC=2.4.1.13;
DE AltName: Full=Sucrose-UDP glucosyltransferase 5;
GN Name=SUS5; OrderedLocusNames=At5g37180; ORFNames=MJG14.25;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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 TISSUE SPECIFICITY, AND DISRUPTION 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 -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:19470642}.
CC -!- TISSUE SPECIFICITY: Detected in the whole plant but more precisely
CC confined to the vasculature in cotyledons, leaves, petals, anthers and
CC roots. Also detected in developing siliques, young immature rosette and
CC cauline leaves. {ECO:0000269|PubMed:14739263,
CC ECO:0000269|PubMed:17257168, ECO:0000269|PubMed:18635527,
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11375.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB017068; BAB11375.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F4K5W8; -.
DR SMR; F4K5W8; -.
DR STRING; 3702.AT5G37180.1; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR PaxDb; F4K5W8; -.
DR PRIDE; F4K5W8; -.
DR ProteomicsDB; 228312; -.
DR Araport; AT5G37180; -.
DR TAIR; locus:2166203; AT5G37180.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_019158_1_0_1; -.
DR InParanoid; F4K5W8; -.
DR BioCyc; MetaCyc:AT5G37180-MON; -.
DR BRENDA; 2.4.1.13; 399.
DR PRO; PR:F4K5W8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K5W8; baseline and differential.
DR Genevisible; F4K5W8; 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 2: Evidence at transcript level;
KW Cell wall; Glycosyltransferase; Reference proteome; Secreted; Transferase.
FT CHAIN 1..836
FT /note="Sucrose synthase 5"
FT /id="PRO_0000418804"
FT REGION 270..748
FT /note="GT-B glycosyltransferase"
FT /evidence="ECO:0000250"
FT REGION 805..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 94905 MW; 761DC9728DFDE252 CRC64;
MEMTSGSLGN GIPEAMGQNR GNIKRCLEKY IENGRRVMKL NELMDEMEIV INDVTQRRRV
MEGDLGKILC FTQAVVIPPN VAFAVRGTPG NWQYVKVNSS NLSVEALSST QYLKLKEFLF
DENWANDENA LEVDFGALDF TLPWLSLSSS IGNGLSFVSS KLGGRLNDNP QSLVDYLLSL
EHQGEKLMMN ETLNTARKLE MSLILADVFL SELPKDTPFQ AFELRFKECG FEKGWGESAG
RVKETMRILS EILQAPDPQN IDRFFARVPR IFNVVIFSVH GYFGQTDVLG LPDTGGQVVY
ILDQVKALED ELLQRINSQG LNFKPQILVV TRLIPDAKKT KCNQELEPIF GTKYSNILRI
PFVTENGILR RWVSRFDIYP YLERFTKDAT TKILDILEGK PDLIIGNYTD GNLVASLMAN
KLGITQATIA HALEKTKYED SDIKWKEFDP KYHFSSQFTA DLISMNSADF IIASTYQEIA
GSKERAGQYE SHMSFTVPGL YRVVSGINVF DPRFNIAAPG ADDSIYFPFT AQDRRFTKFY
TSIDELLYSQ SENDEHIGYL VDKKKPIIFS MARLDVVKNL TGLTEWYAKN KRLRDLVNLV
IVGGFFDASK SKDREEISEI KKMHSLIEKY QLKGQFRWIT AQTDRTRNGE LYRSIADTRG
AFVQPAHYEA FGLTVIEAMS CGLVTFATNQ GGPAEIIVDG VSGFHIDPSN GEESSDKIAD
FFEKSGMDPD YWNMFSNEGL QRINECYTWK IYANKVINMG STYSYWRHLN KDQKLAKQRY
IHSFYNLQYR NLVKTIPILS DIPEPPPLPP KPLVKPSASK GSKRTQPRLS FRLFGA