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Database: UniProt
Entry: A0A1Z5RQI0_SORBI
LinkDB: A0A1Z5RQI0_SORBI
Original site: A0A1Z5RQI0_SORBI 
ID   A0A1Z5RQI0_SORBI        Unreviewed;      1952 AA.
AC   A0A1Z5RQI0;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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_3004G358400 {ECO:0000313|EMBL:OQU86033.1};
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:OQU86033.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:OQU86033.1, 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; CM000763; OQU86033.1; -; Genomic_DNA.
DR   STRING; 4558.A0A1Z5RQI0; -.
DR   EnsemblPlants; OQU86033; OQU86033; SORBI_3004G358400.
DR   Gramene; OQU86033; OQU86033; SORBI_3004G358400.
DR   eggNOG; KOG0916; Eukaryota.
DR   InParanoid; A0A1Z5RQI0; -.
DR   OMA; ITNFQWH; -.
DR   OrthoDB; 211713at2759; -.
DR   Proteomes; UP000000768; Chromosome 4.
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:SF103; 1,3-BETA-GLUCAN SYNTHASE; 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; 1.
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        532..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        566..586
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        611..632
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        672..692
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        721..739
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        745..765
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1513..1535
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1564..1583
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1682..1706
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1760..1778
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1790..1811
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1823..1846
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1852..1872
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1893..1915
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          330..446
FT                   /note="1,3-beta-glucan synthase component FKS1-like"
FT                   /evidence="ECO:0000259|SMART:SM01205"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1952 AA;  225015 MW;  ED27FEF8F4B5B8F8 CRC64;
     MASSSGGGGG RRLAPGGDAS PASAGARRIY RTQTAGNLGD SIFDSEVVPS SLVEIAPILR
     VANEVEASNP RVAYLCRFYA FEKAHRLDPT SSGRGVRQFK TALLQRLERE NDPTLKGRVK
     QSDAREMQSF YQHYYKKYIQ ALQNAADKAD RAQLTKAYQT AAVLFEVLKA VNVSQKIEVD
     QSILETHNQV EEKKKLYLPY NILPLDPDSA NQAIMRYPEI QAAFHALRNT RGLPWPKEHD
     KKPDADLLAW LQAMFGFQKD NVSNQREHLI LLLANVHIRQ IPKPEQQPKL DDRALDTVMK
     KLFKNYKRWC KYLGRKSSLW LPTIQQEVQQ RKLLYMGLYL LIWGEAANLR FMPECLCYIY
     HHMAFELYGM LAGNVSPTTG ENVKPAYGGE EEAFLKRVVT PIYKVIEKEV ERSKTMKSKH
     SHWRNYDDLN EYFWSRDCFR LGWPMRSDAD FFKTPNVSLH HLDGEDRPVG NGNWMGKVNF
     VEIRSFWHIF RSFDRMWSFL ILSLQAMIII AWNGGTPSDI FDRGVFKQVL SIFITAAILK
     LGQAILDIIL SWKARRNMSL VVKLRYILKL LSAAAWVVIL PVTYAYTWEN PTGLARTIKS
     WLGDGQNQPS LYILAVVIYL APNLLSATLF LFPVIRRALE RSNLRVVTFI MWWSQPRLFV
     GRGMHEGAFS LFKYTMFWVL LLATKLVVSF YVEIKPLVQP TKDIMKEPIR TFKWHEFFPH
     ANNNIGVVIA LWAPIILVYF MDTQIWYAIF STLIGGVYGA CRRLGEIRTL GMLRSRFESL
     PKAFNQCLIP SDTSKRRGFR AAFSKPSKTP EDTKEEEKIA ARFAQIWNLI ITSFREEDLI
     DDREKDLLLV PYCKDRDMDI IQWPPFLLAS KIPIALDMAA DSGGKDRDLK KRMKSDPYFT
     YAIKECYASF KNIIYALVIS SRERGFIQKI FDMVDEHITE ETLIKELNMS NLPTLSKKFI
     ELLDLLESNN KEEQGQVIIL FQDMLEVVTR DIMVDQLSDL LESIHGPNNK RSEGMMPLDQ
     QVQLFTKAID FPVKKTQAWN EKIKRLRLLL TVKESAMDVP TNLDARRRIS FFANSLFMSM
     PDAPKVRQML PFSVLTPYYK EDVLFSSQAL GEQNEDGVSI LFYLQKIYPD EWKNFLERVH
     CESEDQLHET EQSEEQLRLW ASYRGQTLTR TVRGMMYYRQ ALVLQAFLDM ARDDDLMEGF
     RAADLLSESD ESQLLTQCKA IADMKFTYVV SCQQYGIQKR SGDPHAQDIL RLMTTYPSLR
     VAYIDEVEEP SKDRNKKIEK VYYSALVKAA VTKPDDPGQK LDQDIYRIKL PGNAMLGEGK
     PENQNHAIIF TRGEGLQTID MNQEHYMEET LKMRNLLQEF LKKHDGVRYP SILGVREHIF
     TGSVSSLAWF MSNQETSFVT IGQRVLANPL RVRFHYGHPD IFDRLFHLTR GGVSKASKII
     NLSEDIFAGF NSTLREGNVT HHEYMQVGKG RDVGLNQISL FEAKIANGNG EQTLSRDVYR
     LGHRFDFFRM LSCYYTTIGF YFSTMITVWT VYVFLYGRLY LVLSGLDEAL ATGKRFIHNE
     PLQVALASQS FVQLGFLMAL PMMMEIGLER GFRTALSDFV LMQLQLASVF FTFSLGTKTH
     YYGTTLLHGG AEYRATGRGF VVFHAKFAEN YRLYSRSHFV KGIELMILLI VYEIFGQSYR
     GAIAYIFITI SMWFMVVTWL FAPFLFNPSG FEWQKIVDDW TDWNKWISNR GGIGVPPEKS
     WESWWEKEQE PLRHSGKRGT VLEIVLALRF FIYQYGLVYH LNITTHTKSV LVYCISWVII
     FVILLVMKTV SVGRRKFSAE FQLVFRLIKG LIFITFISII IILIAIPHMT VQDIFVCILA
     FMPTGWGLLL IAQTMRSAIS HMGLWGSVKA LARGYEIIMG LLLFTPIAFL AWFPFVSEFQ
     TRMLFNQAFS RGLQISRILG GHKKDRAARN KE
//
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