ID K7MDN8_SOYBN Unreviewed; 1965 AA.
AC K7MDN8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
DE AltName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00032165};
GN Name=100799445 {ECO:0000313|EnsemblPlants:KRH13524};
GN ORFNames=GLYMA_15G245800 {ECO:0000313|EMBL:KRH13524.1};
OS Glycine max (Soybean) (Glycine hispida).
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; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH13524.1};
RN [1] {ECO:0000313|EMBL:KRH13524.1, ECO:0000313|EnsemblPlants:KRH13524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH13524};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH13524.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH13524}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH13524};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH13524.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH13524.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC Evidence={ECO:0000256|ARBA:ARBA00000192};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000256|ARBA:ARBA00009040}.
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DR EMBL; CM000848; KRH13524.1; -; Genomic_DNA.
DR RefSeq; XP_006598152.1; XM_006598089.2.
DR AlphaFoldDB; K7MDN8; -.
DR SMR; K7MDN8; -.
DR STRING; 3847.K7MDN8; -.
DR PaxDb; 3847-GLYMA15G39420-2; -.
DR EnsemblPlants; KRH13524; KRH13524; GLYMA_15G245800.
DR GeneID; 100799445; -.
DR Gramene; KRH13524; KRH13524; GLYMA_15G245800.
DR KEGG; gmx:100799445; -.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000742_0_0_1; -.
DR InParanoid; K7MDN8; -.
DR OMA; RMGCENL; -.
DR OrthoDB; 211713at2759; -.
DR Proteomes; UP000008827; Chromosome 15.
DR ExpressionAtlas; K7MDN8; baseline and differential.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.270; Vacuolar protein sorting-associated protein vta1; 1.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR InterPro; IPR039431; Vta1/CALS_N.
DR InterPro; IPR023175; Vta1/CALS_N_sf.
DR PANTHER; PTHR12741:SF22; CALLOSE SYNTHASE 8-RELATED; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 2.
DR Pfam; PF04652; Vta1; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 524..541
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 553..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..659
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 698..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 772..791
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1531..1553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1589..1606
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1618..1635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1704..1723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1807..1824
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1844..1864
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1871..1892
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1912..1933
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 331..447
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 473..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1965 AA; 227404 MW; 2F02E1968D0D7FD7 CRC64;
MSEIVPAEPI GGIYFEPGET STATASASEA PRVTLAITNG SNTVEYVPEP FDSERLPTVF
ASEIQRFLRV ANLLGKEEPR VAYLCRVHAF VIAHNLDKNS SGRGVRQFKT SLLHRLEQDE
HVTKKKGTSD IRELKNVYRA YRDYYIRHEK AFDLEQSRRE RLINARDIAT VLFEVLKTVT
DPASSQALIQ GNAIHKKTEF NILPLEQGGI QHAITQKSEI KAAVAVIRNV RGLPPAQDFK
KHGAFVDLFD FLQHCFGFQE ANVANQREHL ILLLANMQTR QTHNQTSVLK LGEGGVDELM
RKFFKNYTNW CKFLERKSNI RLPLVKQESQ QYKILYIGLY LLIWGEAANL RFMPECLCYI
FHHMAYELHG ILCGAISLTT WEKVMPAYGG EPESFLNNVV TRIYTVIKQE VDNSKGGAAD
YSVWRNYDDL NEYFWSPDCF KIGWPMRLDH EFFFVKSRNK PKPDVKNALV VSPGKTKEKK
KREKRDEEEP EDTREEIHEP QWLGKTNFVE IRSFWQIFRC FDRMWSFFIL SLQAIIIIAC
HDLGSPIQLL DAVVFEDIIT IFITSAYLKL IQAILDIAFM WKARYTMEYS QKVKLVVKLV
LATIWTIVLP VCYANSRRKY TCYSTKYGSL VEEWCFTSYM VAAAIYLTTN AVEVVLFFVP
AVAKYIEVSN YKICRVLSWW TQPRIYVGRG MQEDQVSVLK YTLFWILVLS CKFVFSYSFE
VKPLIAPTRQ IMKIGVKKYE WHELFPKVKS NAGAIVAVWS PVVIVYFMDT QIWYSVFCTI
IGGLYGVLHH LGEIRTLGML RSKFDSLPSA FNVCLIPPSS KRGKKKRKGL LSNIFQKLPD
EKNATAKFVV VWNQIVNHLR LEDLISNREM DLMMMPVSSE LFSAKVRWPV FLLANKFSTA
LTIAKDFEGK EEILVKKITK DKYMFYAVRE CYQSLKYVLE ILVVGSIEKR IICDILSEIE
KHIQETSLLK NFNLKVLPAL HAKVVELAEL LMEGDKDHQH KVVKALLDVF ELVTNDMMVD
SRILDMFHFP EQNECGFVYF RNDDQLFDSV EMNRDFYPFA NENSIHFPLP ESGPLMEKIK
RFHLLLTVKD TAMDVPANLD ARRRISFFAT SLFTDMPDAP KVHNMMPFCV ITPHYIEDIN
FSLKELGSDK EEDSIIFYMQ KIYPDEWTNF LERMGCDNRK SLEDEHKTED LRLWASFRGQ
TLSRTVRGMM YYREALKLQA FLDMAEEEDI LEGYETAERG NRALFARLEA LADMKYTYVI
SCQSFASQKA SNDPRYQDMI DLMIRYPSLR VAYVEEKEEI VQGKPHKVYS SKLVKVVNGF
EQTIYQIKLP GTPHLGEGKP ENQNNAIIFT RGEALQTIDM NQDNYLEEAL KMRNLLQEFL
QRQGRRPPTI LGLREHIFTG SVSSLAWFMS YQETSFVTIG QRLLANPLRV RFHYGHPDVF
DRVFHITRGG ISKASKTINL SEDVFAGFNS TLRRGCISYH EYLQIGKGRD VALNQISKFE
AKVANGNCEQ TISRDMFRLG RQFDFFRMLS CYFTTIGFYF SSLISVIGIY VFLYGQLYLV
LSGLERALII EARIKNVQSL ETALASQSFI QLGLLTGLPM VMEIGLERGF LTALKDFVLM
QLQLAAVFFT FALGTKTHYY GRTLLHGGAK YRPTGRKVVF HASFTENYRL YSRSHFVKAF
ELLLLLIVYN MFRRSYQSSM AYVLITYAIW FMSLTWLCAP FLFNPAGFSW TKTVDDWKEW
NKWIRQQGGI GIQQDKSWHS WWHDEQAHLR WSGFGSRLTE VLLSLRFFIY QYGLVYHLDI
SQHSKNFLVY VLSWIVIVAI FLLVKAVNMG RQLLSANYQL GFRFFKAFLF LAVLAIIFTL
SIICELSLTD LFVCCLAFMP TAWGLIMMAQ AARPKIEHTG LWDFTRALAR EFDYGMGIVL
FGPIAILAWL PIIKAFHARF LFNEAFKRHL QIQPILAGKK KKHRT
//
