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GOLS7_ARATH
ID   GOLS7_ARATH             Reviewed;         332 AA.
AC   Q4PSY4; O80766;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Galactinol synthase 7;
DE            Short=AtGolS7;
DE            Short=GolS-7;
DE            EC=2.4.1.123;
GN   Name=GOLS7; OrderedLocusNames=At1g60450; ORFNames=T13D8.32;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA   Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GENE FAMILY.
RX   PubMed=11846875; DOI=10.1046/j.0960-7412.2001.01227.x;
RA   Taji T., Ohsumi C., Iuchi S., Seki M., Kasuga M., Kobayashi M.,
RA   Yamaguchi-Shinozaki K., Shinozaki K.;
RT   "Important roles of drought- and cold-inducible genes for galactinol
RT   synthase in stress tolerance in Arabidopsis thaliana.";
RL   Plant J. 29:417-426(2002).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18502973; DOI=10.1104/pp.108.122465;
RA   Nishizawa A., Yabuta Y., Shigeoka S.;
RT   "Galactinol and raffinose constitute a novel function to protect plants
RT   from oxidative damage.";
RL   Plant Physiol. 147:1251-1263(2008).
CC   -!- FUNCTION: Galactinol synthase involved in the biosynthesis of raffinose
CC       family oligosaccharides (RFOs) that function as osmoprotectants. May
CC       promote plant stress tolerance (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=myo-inositol + UDP-alpha-D-galactose = alpha-D-galactosyl-
CC         (1->3)-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:12464,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17268, ChEBI:CHEBI:17505,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.123;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC       Galactosyltransferase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC24075.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC004473; AAC24075.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE33688.1; -; Genomic_DNA.
DR   EMBL; DQ056502; AAY78659.1; -; mRNA.
DR   PIR; T02295; T02295.
DR   RefSeq; NP_176248.1; NM_104732.2.
DR   AlphaFoldDB; Q4PSY4; -.
DR   SMR; Q4PSY4; -.
DR   STRING; 3702.AT1G60450.1; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   PaxDb; Q4PSY4; -.
DR   PRIDE; Q4PSY4; -.
DR   ProteomicsDB; 247019; -.
DR   EnsemblPlants; AT1G60450.1; AT1G60450.1; AT1G60450.
DR   GeneID; 842340; -.
DR   Gramene; AT1G60450.1; AT1G60450.1; AT1G60450.
DR   KEGG; ath:AT1G60450; -.
DR   Araport; AT1G60450; -.
DR   TAIR; locus:2195668; AT1G60450.
DR   eggNOG; KOG1950; Eukaryota.
DR   HOGENOM; CLU_049943_3_0_1; -.
DR   InParanoid; Q4PSY4; -.
DR   OMA; EEPNMDR; -.
DR   OrthoDB; 818680at2759; -.
DR   PhylomeDB; Q4PSY4; -.
DR   PRO; PR:Q4PSY4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q4PSY4; baseline and differential.
DR   Genevisible; Q4PSY4; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0047216; F:inositol 3-alpha-galactosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006012; P:galactose metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR002495; Glyco_trans_8.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01501; Glyco_transf_8; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cytoplasm; Galactose metabolism;
KW   Glycosyltransferase; Manganese; Metal-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..332
FT                   /note="Galactinol synthase 7"
FT                   /id="PRO_0000418663"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   332 AA;  37768 MW;  224762F3C6984DC6 CRC64;
     MTPETHVDMI NASEKAPKER AYVTFLAGNG DYVKGVVGLA KGLRKVKSAY PLVVAMLPDV
     PEEHREILRS QGCIVREIEP VHPPDSQDAY ARAYYIINYS KLRIWNFEEY NKMIYLDADI
     QVFGNIDDLF DMQDGYLHGV LSCFCEKIWS YTPLYSIGYC QYCPEKVVWP AEMESAPPSP
     YFNAGMFVFE PNPLTYESLL QTLQVTPPTP FAEQDFLNMF FGKVFKPVSP VYNLILSVLW
     RHPGKVDLES VKVVHYCPPG SKPWRYTGEE PNMDREDVKM LIKKWWDIYN DESLDFKPKS
     PADLEATVLE STIIASVTEA PLSYSPAAPS AA
 
 
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