CSLA1_CYATE
ID CSLA1_CYATE Reviewed; 526 AA.
AC Q6UDF0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Glucomannan 4-beta-mannosyltransferase 1 {ECO:0000305};
DE EC=2.4.1.32 {ECO:0000269|PubMed:14726589};
DE AltName: Full=CtManS {ECO:0000303|PubMed:14726589};
DE AltName: Full=Glucomannan synthase {ECO:0000305};
DE AltName: Full=Mannan synthase 1 {ECO:0000305};
GN Name=ManS {ECO:0000303|PubMed:14726589};
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], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=14726589; DOI=10.1126/science.1090908;
RA Dhugga K.S., Barreiro R., Whitten B., Stecca K., Hazebroek J.,
RA Randhawa G.S., Dolan M., Kinney A.J., Tomes D., Nichols S., Anderson P.;
RT "Guar seed beta-mannan synthase is a member of the cellulose synthase super
RT gene family.";
RL Science 303:363-366(2004).
CC -!- FUNCTION: Possesses 4-beta-mannosyltransferase activity on mannan using
CC GDP-mannose. The beta-1,4-mannan product is the backbone for
CC galactomannan synthesis by galactomannan galactosyltransferase. The
CC galactomannan is a hemicellulosic storage polysaccharide accumulated in
CC the form of secondary wall thickenings in the seed endosperm.
CC {ECO:0000269|PubMed:14726589}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-mannose + (glucomannan)n = GDP + (glucomannan)n+1.;
CC EC=2.4.1.32; Evidence={ECO:0000269|PubMed:14726589};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:14726589}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14726589}.
CC -!- DEVELOPMENTAL STAGE: Expressed exclusively in the endosperm of
CC developing seeds, 25 to 30 days after flowering. Not expressed in the
CC embryo or seed coat. {ECO:0000269|PubMed:14726589}.
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 non-food
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 2 family. Plant
CC cellulose synthase-like A subfamily. {ECO:0000305}.
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DR EMBL; AY372247; AAR23313.1; -; mRNA.
DR AlphaFoldDB; Q6UDF0; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
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:0047259; F:glucomannan 4-beta-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF13632; Glyco_trans_2_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Golgi apparatus;
KW Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..526
FT /note="Glucomannan 4-beta-mannosyltransferase 1"
FT /id="PRO_0000319381"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 130
FT /evidence="ECO:0000255"
FT ACT_SITE 283
FT /evidence="ECO:0000255"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 526 AA; 60677 MW; EF512855ACAF247F CRC64;
MRNLIFEEPE GIPGNSSSSL RYAWQSIRAP VIIPLLKLAV IVCSVMSIML FVERVAMAAV
ILIVKVLRKK RYTKYNLEAM KQKLERSKKY PMVLIQIPMY NEKEVYKLSI GAVCGLSWPA
DRFIVQVLDD STNPVLRELV EMECQKWIQK GVNVKYENRR NRNGYKAGAL KEGLEKQYVE
DCEFVAIFDA DFQPDADFLW NTIPYLLENP KLGLVQARWK FVNSEECMMT RLQEMSLDYH
FSVEQEVGSS TYSFFGFNGT AGVWRIQAIK DAGGWKDRTT VEDMDLAVRA SLHGWEFVFV
GDVKVKNELP STFKAYRFQQ HRWSCGPANL FKKMTKEIIC CKRVPLLKRL HLIYAFFFVR
KIVAHWVTFF FYCIVIPACV IVPEVNLKKQ IAIYIPATIT ILNAVSTPRS MHLLVLWILF
ENVMSLHRTK AAIIGLLEAN RVNEWVVTEK LGNAMKQRNN ARPSRASRFR IIERIHPLEI
IVGMYMLHCA TYDLLFGHDH FFVYLLLQAG AFFTMGFGLV GTIVPT
