SUS4_ARATH
ID SUS4_ARATH Reviewed; 808 AA.
AC Q9LXL5; Q0WT99; Q94CC8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Sucrose synthase 4;
DE Short=AtSUS4;
DE EC=2.4.1.13;
DE AltName: Full=Sucrose-UDP glucosyltransferase 4;
GN Name=SUS4; OrderedLocusNames=At3g43190; ORFNames=F7K15_40;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-395.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-808.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, TISSUE SPECIFICITY, AND INDUCTION.
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 [6]
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION, AND
RP 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 [7]
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 [8]
RP INDUCTION BY NUC.
RX PubMed=21265895; DOI=10.1111/j.1365-313x.2010.04432.x;
RA Seo P.J., Ryu J., Kang S.K., Park C.M.;
RT "Modulation of sugar metabolism by an INDETERMINATE DOMAIN transcription
RT factor contributes to photoperiodic flowering in Arabidopsis.";
RL Plant J. 65:418-429(2011).
CC -!- FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and
CC fructose for various metabolic pathways. {ECO:0000250}.
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=4.97 mM for D-fructose (synthetic reaction) at pH 9.4
CC {ECO:0000269|PubMed:17257168};
CC KM=0.07 mM for UDP-glucose (synthetic reaction) at pH 9.4
CC {ECO:0000269|PubMed:17257168};
CC KM=67.54 mM for sucrose (degradative reaction) at pH 6
CC {ECO:0000269|PubMed:17257168};
CC KM=0.07 mM for UDP (degradative reaction) at pH 6
CC {ECO:0000269|PubMed:17257168};
CC Vmax=12.01 umol/min/mg enzyme for synthetic reaction at pH 9.4
CC {ECO:0000269|PubMed:17257168};
CC Vmax=4.99 umol/min/mg enzyme for degradative reaction at pH 6
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 -!- TISSUE SPECIFICITY: Detected in the whole plant with highest expression
CC in young rosette leaves and roots. {ECO:0000269|PubMed:14739263,
CC ECO:0000269|PubMed:17257168, ECO:0000269|PubMed:18635527}.
CC -!- INDUCTION: By anaerobic stress. By hypoxia in the roots (at protein
CC level). Up-regulated by NUC/IDD8. {ECO:0000269|PubMed:14739263,
CC ECO:0000269|PubMed:17257168, ECO:0000269|PubMed:21265895}.
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=AAK59464.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL353871; CAB89040.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77773.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64625.1; -; Genomic_DNA.
DR EMBL; AK227662; BAE99649.1; -; mRNA.
DR EMBL; AY034958; AAK59464.1; ALT_INIT; mRNA.
DR PIR; T49233; T49233.
DR RefSeq; NP_001326640.1; NM_001339091.1.
DR RefSeq; NP_566865.2; NM_114187.5.
DR AlphaFoldDB; Q9LXL5; -.
DR SMR; Q9LXL5; -.
DR BioGRID; 8715; 2.
DR STRING; 3702.AT3G43190.1; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; Q9LXL5; -.
DR MetOSite; Q9LXL5; -.
DR SwissPalm; Q9LXL5; -.
DR PaxDb; Q9LXL5; -.
DR PRIDE; Q9LXL5; -.
DR ProteomicsDB; 234102; -.
DR EnsemblPlants; AT3G43190.1; AT3G43190.1; AT3G43190.
DR EnsemblPlants; AT3G43190.2; AT3G43190.2; AT3G43190.
DR GeneID; 823393; -.
DR Gramene; AT3G43190.1; AT3G43190.1; AT3G43190.
DR Gramene; AT3G43190.2; AT3G43190.2; AT3G43190.
DR KEGG; ath:AT3G43190; -.
DR Araport; AT3G43190; -.
DR TAIR; locus:2084756; AT3G43190.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_019158_1_0_1; -.
DR InParanoid; Q9LXL5; -.
DR OMA; SYSAFEH; -.
DR OrthoDB; 153947at2759; -.
DR PhylomeDB; Q9LXL5; -.
DR BioCyc; MetaCyc:AT3G43190-MON; -.
DR BRENDA; 2.4.1.13; 399.
DR PRO; PR:Q9LXL5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LXL5; baseline and differential.
DR Genevisible; Q9LXL5; AT.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0016157; F:sucrose synthase activity; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0001666; P:response to hypoxia; IEP:UniProtKB.
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 Glycosyltransferase; Reference proteome; Stress response; Transferase.
FT CHAIN 1..808
FT /note="Sucrose synthase 4"
FT /id="PRO_0000418803"
FT REGION 277..754
FT /note="GT-B glycosyltransferase"
FT /evidence="ECO:0000250"
FT CONFLICT 395
FT /note="D -> V (in Ref. 3; BAE99649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 808 AA; 93003 MW; C9FDF33B6325CFBB CRC64;
MANAERVITR VHSQRERLDA TLVAQKNEVF ALLSRVEAKG KGILQHHQII AEFEAMPLET
QKKLKGGAFF EFLRSAQEAI VLPPFVALAV RPRPGVWEYV RVNLHDLVVE ELQASEYLQF
KEELVDGIKN GNFTLELDFE PFNAAFPRPT LNKYIGDGVE FLNRHLSAKL FHDKESLHPL
LKFLRLHSHE GKTLMLNNRI QNLNTLQHNL RKAEEYLMEL KPETLYSEFE HKFQEIGLER
GWGDTAERVL NMIRLLLDLL EAPDPCTLEN FLGRIPMVFN VVILSPHGYF AQDNVLGYPD
TGGQVVYILD QVRALETEML QRIKQQGLNI TPRILIITRL LPDAAGTTCG QRLEKVYGSQ
YCDILRVPFR TEKGIVRKWI SRFEVWPYLE TFTEDVAAEI SKELQGKPDL IIGNYSDGNL
VASLLAHKLG VTQCTIAHAL EKTKYPDSDI YWKKLDEKYH FSCQFTADLI AMNHTDFIIT
STFQEIAGSK DTVGQYESHR SFTLPGLYRV VHGIDVFDPK FNIVSPGADM SIYFAYTEEK
RRLTAFHLEI EELLYSDVEN EEHLCVLKDK KKPIIFTMAR LDRVKNLSGL VEWYGKNTRL
RELVNLVVVG GDRRKESQDN EEKAEMKKMY ELIEEYKLNG QFRWISSQMN RVRNGELYRY
ICDTKGAFVQ PALYEAFGLT VVEAMTCGLP TFATCNGGPA EIIVHGKSGF HIDPYHGDKA
AESLADFFTK CKHDPSHWDQ ISLGGLERIQ EKYTWQIYSQ RLLTLTGVYG FWKHVSNLDR
LESRRYLEMF YALKYRPLAQ AVPLAHEE
