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SUS1_DAUCA
ID   SUS1_DAUCA              Reviewed;         808 AA.
AC   P49035;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Sucrose synthase isoform 1;
DE            EC=2.4.1.13;
DE   AltName: Full=Sucrose synthase isoform I;
DE   AltName: Full=Sucrose-UDP glucosyltransferase 1;
DE   AltName: Full=Susy*Dc1;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nantaise;
RX   PubMed=7784526; DOI=10.1104/pp.108.1.75;
RA   Sebkova V., Unger C., Hardegger M., Sturm A.;
RT   "Biochemical, physiological, and molecular characterization of sucrose
RT   synthase from Daucus carota.";
RL   Plant Physiol. 108:75-83(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Nantaise; TISSUE=Leaf;
RX   PubMed=10080700; DOI=10.1023/a:1006199003756;
RA   Sturm A., Lienhard S., Schatt S., Hardegger M.;
RT   "Tissue-specific expression of two genes for sucrose synthase in carrot
RT   (Daucus carota L.).";
RL   Plant Mol. Biol. 39:349-360(1999).
CC   -!- FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and
CC       fructose for various metabolic pathways.
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   -!- ACTIVITY REGULATION: Fructose acts as a non-competitive inhibitor with
CC       an inhibition constant of 17.2 mM. In contrast, glucose inhibits
CC       uncompetitively with an inhibition constant of 4.3 mM.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- TISSUE SPECIFICITY: Expressed in stems, in roots at different
CC       developmental stages, and in flower buds, flowers and maturing seeds,
CC       with the highest levels in strong utilization sinks for sucrose such as
CC       growing stems and tap root tips.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. Plant sucrose
CC       synthase subfamily. {ECO:0000305}.
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DR   EMBL; X75332; CAA53081.1; -; mRNA.
DR   EMBL; Y16090; CAA76056.1; -; Genomic_DNA.
DR   PIR; S37560; S37560.
DR   AlphaFoldDB; P49035; -.
DR   SMR; P49035; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PRIDE; P49035; -.
DR   SABIO-RK; P49035; -.
DR   GO; GO:0016157; F:sucrose synthase activity; IEA:UniProtKB-EC.
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   Glycosyltransferase; Transferase.
FT   CHAIN           1..808
FT                   /note="Sucrose synthase isoform 1"
FT                   /id="PRO_0000204647"
FT   REGION          277..754
FT                   /note="GT-B glycosyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:P49040"
SQ   SEQUENCE   808 AA;  92474 MW;  1A40FCABAA4A5425 CRC64;
     MGEPVLTRVH SLRERMDSTL ANHRNEILMF LSRIESHGKG ILKPHQLLAE YEAISKEDKL
     KLDDGHGAFA EVIKSTQEAI VSPPWVALAI RLRPGVWEYV RVNVHHLVVE ELSVPQYLQF
     KEELVIGSSD ANFVLELDFA PFTASFPRPT LTKSIGNGVE FLNRHLSAKM FHGKDSMHPL
     LEFLRLHNYN GKTLMLNNRV QNVNGLQSML RKAGDYLSTL PSDTPYSEFE HKFQEIGFER
     GWGDTAERVT EMFHMLLDLL EAPDASTLET FLGKIPMVFN VVILSPHGYF AQENVLGYPD
     TGGQVVYILD QVPALEREMI KRIKEQGLDI KPRILIVTRL LPDAVGTTCN QRLEKVFGAE
     HAHILRVPFR TEKGILRKWI SRFEVWPYIE TFTEDVAKEI ALELQAKPDL IIGNYSEGNL
     VASLLAHKLG VTQCTIAHAL EKTKYPDSDI YWEKFDKKYH FSSQFTADLI AMNHTDFIIT
     STFQEIAGSK DTVGQYESHT AFTMPGLYRV VHGIDVFDPK FNIVSPGADT SVYFSYKEKE
     KRLTTLHPEI EELLYSSVEN EEHLCIIKDK NKPILFTMAR LDNVKNLTGF VEWYAKSPKL
     RELVNLVVVG GDRRKESKDL EEQAQMKKMY ELIDTYKLNG QFRWISSQMN RVRNGELYRY
     IADTKGAFVQ PAFYEAFGLT VVEAMTCGLP TFATLHGGPA EIIVHGKSGF HIDPYHGEQV
     AELLVNFFEK CKTDPSQWDA ISAGGLKRIQ EKYTWQIYSE RLLTLAGVYG FWKHVSKLDR
     LEIRRYLEMF YALKYRKLAE SVPLAKDE
 
 
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