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Database: UniProt
Entry: C5XM95_SORBI
LinkDB: C5XM95_SORBI
Original site: C5XM95_SORBI 
ID   C5XM95_SORBI            Unreviewed;      1934 AA.
AC   C5XM95;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 2.
DT   27-MAR-2024, entry version 49.
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   ORFNames=SORBI_3003G179600 {ECO:0000313|EMBL:EES03079.2};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:EES03079.2, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:EES03079.2, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(2018).
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; CM000762; EES03079.2; -; Genomic_DNA.
DR   STRING; 4558.C5XM95; -.
DR   EnsemblPlants; EES03079; EES03079; SORBI_3003G179600.
DR   Gramene; EES03079; EES03079; SORBI_3003G179600.
DR   eggNOG; KOG0916; Eukaryota.
DR   HOGENOM; CLU_3093705_0_0_1; -.
DR   InParanoid; C5XM95; -.
DR   OMA; WCPENGA; -.
DR   OrthoDB; 211713at2759; -.
DR   Proteomes; UP000000768; Chromosome 3.
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:SF16; CALLOSE SYNTHASE 7; 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:UP000000768};
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        515..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        545..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        586..609
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        629..652
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        695..716
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        763..782
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1495..1517
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1553..1571
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1642..1661
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1667..1689
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1742..1761
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1773..1793
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1814..1835
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1841..1861
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1881..1898
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          342..457
FT                   /note="1,3-beta-glucan synthase component FKS1-like"
FT                   /evidence="ECO:0000259|SMART:SM01205"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1934 AA;  224136 MW;  EED2966C8A4244E3 CRC64;
     MASGGAGPSG PVRSTSQTRQ RTMGRIPTRA YTMRPDGLSG EDGPGFEEEE LVPSSLAPIV
     PILRAANEIE EENPRVAYLC RFTAFEKAHL MDPISGGRGV RQFKTYLLHR LEKDEHETNR
     RLATTDAKEI QRFYEQYCKK YLEEGHDKRK PEEMARHYQI ASVLYDVLKT VTPGKNEYDK
     YAKGVEKEKA SFSQYNILPL NISTPRQPIM EIPEIKAAVA LLRQMDDLPM PRIELTQSSD
     GKTVPDEMDK PLVQDLLDWL WQTFGFQKGN VENQKEHLIL LLANIDMRQQ GTSHHSGRHV
     HVIHSSTVIY LMDKIFQNYN SWCRYLHLDS NIIIASDAST QRPELLYIGL YLLIWGEASN
     VRFMPECLCY IFHHMARDLH DIISDRREGP FEPPFQREGS DDAFLQLVIQ PIYSVMQKEA
     ARGKHGTVSH SMWRNYDDLN EYFWSKKCFK KLGWPMNPTA DFFADTRATN ETEQHDHVIS
     RRRQHDHVIS RRRASKTNFV EVRTFLHLFR SFDRMWAFFI LAFQAMVIIA WSSSGALSSI
     FEPEVFRNVL TIFITAAFLN FLQATLEIIL NWKAWKSLEC SQRIRYILKF AVAVAWLIIL
     PTTYSSSIQN PTGLVKFVSN WINLQNESIY NYAVALYMLP NIFSALFFMF LPIRRVLERS
     NSRIIRFLLW WTQPKLYVAR GMYEDTCSLL KYTTFWILLL ICKLAFSYYV EIAPLVEPTR
     IIMSLERPPY EWHEFFPNLR HNLGVVVTVW APIVMVYFMD TQIWYAIFST ICGGVYGAFS
     RLGEIRTLGM LRSRFEAIPR AFGKKLVPNH GSRLKRDEED KNPPFDKFAD IWNAFINSLR
     EEDLLSNREK NLLVVPSSGG ETSVFQWPPF LLASKIPIAL DMAKSVKKKD EELMKRIKQD
     PYTEYAVIEC YETLLDILYS IIVEQSDKKV VDRICESIKD SIHRRSLVKE FRLDELPQLS
     VKFDKLLDLL KKYDENDPVN NNTQIANLLQ DIMEIITQDI MKNGQGILKD EGQKQLFANL
     NLDSLKDVAW KEKCIRLQLL LTTKESAIYV PTNLEARRRI TFFANSLFMK MPRAPPVRSM
     MSFSVLTPYF KEEVLFSPED LRKKNEDGIS ILFYLRKIYP DEFRNFLERI DFKPKDEEEL
     KDRMDEICPW ASYRGQTLTR TVRGMMYYRK ALEIQCLQDT KDPAKFDQDG LIESYRELQS
     SIEMAQAIAD IKFTYVVSCQ VYGMQKTSKD SKDKSRYQNI LNLMIINPSL RVAFIDEVEA
     PTGNGATEKT YYSVLVKGGE KYDEEIYRIK LPGKPTDIGE GKPENQNHAI IFTRGEALQA
     IDMNQDNYIE EAFKMRNVLE EFESRKYGKS EPTILGLREH IFTGSVSSLA WFMSNQETSF
     VTIGQRVLAN PLKVRFHYGH PDIFDRLFHI TRGGISKASK TINLSEDIFS GFNSTMRGGN
     VTHHEYMQVG KGRDVGMNQI SSFEAKVANG NGEQTLSRDI YRLGRRFDFY RMLSFYFTTV
     GFYFSSMVTV LTVYVFLYGR LYLVMSGLER SIMLDARNQQ NVKALENALA SQSIFQLGLL
     LVLPMVMEVG LEKGFRTALG EFVIMQLQLA SVFFTFQLGT KTHYYGRTIL HGGAKYRPTG
     RGFVVYHAKF AENYRMYSRS HFVKGLELLI LLVVYLVYGR SYRSSSLYLF VTCSMWFLVA
     SWLFAPFIFN PSCFEWQKTV DDWTDWRKWM GNRGGIGMSV EQSWEAWWLS EQDHLRKTSI
     RALLLEIILS LRFLIYQYGI VYHLNIADHH KSIMVYGVSW VVMLLVLVVL KMVSIGRQKF
     GTDLQLMFRI LKGLLFLGFV SVMAVLFVVL HLTISDVFAS ILGYLPTGWC LLLIGQACSP
     LIRRTMLWDS IMELGRSYEN IMGLILFLPI GFLSWFPFVS EFQTRLLFNQ AFSRGLQISR
     ILAGQKGIGE FEFE
//
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