GMGT1_CYATE
ID GMGT1_CYATE Reviewed; 435 AA.
AC Q564G7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Galactomannan galactosyltransferase 1;
DE EC=2.4.1.-;
GN Name=GMGT1;
OS Cyamopsis tetragonoloba (Guar) (Cluster bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Indigofereae; Cyamopsis.
OX NCBI_TaxID=3832;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seed endosperm;
RA Reid J.S.G., Edwards M.E., Dickson C.A., Gidley M.J., Clark A.H.;
RT "In vitro galactomannan biosynthesis in tobacco transgenic lines expressing
RT legume seed galactomannan galactosyltransferases (GMGTs).";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=14988472; DOI=10.1104/pp.103.029967;
RA Edwards M.E., Choo T.-S., Dickson C.A., Scott C., Gidley M.J., Reid J.S.G.;
RT "The seeds of Lotus japonicus lines transformed with sense, antisense, and
RT sense/antisense galactomannan galactosyltransferase constructs have
RT structurally altered galactomannans in their endosperm cell walls.";
RL Plant Physiol. 134:1153-1162(2004).
CC -!- FUNCTION: Galactomannan galactosyltransferase (GMGT) involved in
CC galactomannan biosynthesis in seed endosperm. GMGT specificity is an
CC important factor regulating the distribution and amount of alpha-1,6-
CC galactose (Gal) substitution of the beta-1,4-linked mannan backbone.
CC {ECO:0000269|PubMed:14988472}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- BIOTECHNOLOGY: Guar gum also called guaran is a galactomannan extracted
CC from guar seed endosperm. Gums are most commonly used as food additives
CC to provide stiffness and texture, prevent ice crystal formation,
CC maintain crispiness, and retain moisture. They have many other nonfood
CC applications such as dying and printing aids in the textile industry,
CC thickeners for shampoos and conditioners, binders and hardeners for
CC paper, rheological facilitators for concrete, and drilling agents for
CC oil and gas wells.
CC -!- MISCELLANEOUS: Galactomannan is accumulated only in the endosperm and
CC constitutes more than 90% of this tissue at maturity. Galactomannan is
CC made by the combined actions of two enzymes: mannan synthase (ManS),
CC which makes beta-1,4-linked mannan backbone, and alpha-
CC galactosyltransferase, which adds galactosyl residues to the mannan
CC backbone. The mannose/galactose ratio of guar galactomannan is 2. The
CC degree of galactosyl substitution on the mannan backbone determines the
CC quality of galactomannan as a gum. A mannose/galactose ratio of 4
CC provides a gum of higher quality than a ratio of 2.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 34 family.
CC {ECO:0000305}.
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DR EMBL; AJ938067; CAI79402.1; -; mRNA.
DR AlphaFoldDB; Q564G7; -.
DR SMR; Q564G7; -.
DR CAZy; GT34; Glycosyltransferase Family 34.
DR PRIDE; Q564G7; -.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR008630; Glyco_trans_34.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR31311; PTHR31311; 1.
DR Pfam; PF05637; Glyco_transf_34; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Coiled coil; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..435
FT /note="Galactomannan galactosyltransferase 1"
FT /id="PRO_0000319356"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..435
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 321..354
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 435 AA; 50956 MW; F5402E419087B979 CRC64;
MAKFGSRNKS PKWISNGCCF LLGAFTALLL LWGLCSFIIP IPNTDPKLNS VATSLRSLNF
PKNPAATLPP NLQHDPPDTT FYDDPETSYT MDKPMKNWDE KRKEWLLHHP SFGAAARDKI
LLVTGSQPKR CHNPIGDHLL LRFFKNKVDY CRLHNYDIIY NNALLHPKMN SYWAKYPVIR
AAMMAHPEVE WVWWVDSDAV FTDMEFKLPL KRYKNHNLVV HGWEGLVRLN HSWTGLNAGV
FLIRNCQWSL EFMDVWVSMG PQTPEYEKWG ERLRETFKDK VLPDSDDQTA LAYLIATDNK
DTWREKIFLE SEYYFEGYWL EIVKTYENIS ERYDEVERKV EGLRRRHAEK VSEKYGAMRE
EYLKDNKRRP FITHFTGCQP CNGHHNPAYN ANDCWNGMER ALNFADNQIL RTYGYHRQNL
LDKSVSPLPF GYPAA