ID A0A200R350_9MAGN Unreviewed; 1899 AA.
AC A0A200R350;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=BVC80_7879g5 {ECO:0000313|EMBL:OVA17115.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA17115.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA17115.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA17115.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OVA17115.1}.
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DR EMBL; MVGT01000453; OVA17115.1; -; Genomic_DNA.
DR STRING; 56857.A0A200R350; -.
DR InParanoid; A0A200R350; -.
DR OrthoDB; 211713at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
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:UP000195402};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OVA17115.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 497..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 565..586
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..633
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 672..693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 724..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1457..1479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1514..1532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1539..1559
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1628..1646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1734..1756
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1777..1802
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1808..1825
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1845..1865
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 333..448
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1899 AA; 220673 MW; 4593358E5326F885 CRC64;
MASSSGTKNE TPSRNLSRRM TRAATMLDVP EDDTTAVDSE LVPSSLASIV PILRVANEIE
PENPRVAYLC RFHAFEKTHK LDPKSSGRGV RQFKTYLLHR LEKVEDVETA PKLAKSDPRE
IQRFYQRFYE ENIKDGVHNK KPEEMAKLYQ IASVLYDVLK SMVPTDKVDD EVNTYAKEVE
KKKEHYAHYN ILPLDALGTP PPIMELPEIK AALNALRKVD NLPKPRLQST VDASHKGLIH
EEEEGDRIVR DLLDWLWLVF GFQKGNVANQ REHLILLLAN VDIRNKHPEN YVQLDSHTVK
HLMDKFFKNY RSWCAYLHCG SNLKFPNNAD RQQLELLYIG LYLLIWGEAS NVRFMPECIC
YIFHNMANEL YGIVFGNVHS VSGEAFQTAY HGEESFLREV ITPIYHVMRK EARRNKGGTT
SHSKWRNYDD LNEYFWYDKC FKLGWPMDHG ADFFVHSEDT HPTNERPNQV VAGKRKPKTN
FVEIRTFWHL FRSFDRMWIF FILAFQAMVI VAWSPSGSPV ALFDEDVFRS VMSIFITWAL
LNFLQATLDI ILSWKAWGSM KYTQIVRYLL KFAVAVVWVI VMPISYSSSV QNPTGLVKFF
SGWIDNWQNQ PLYNYVVAIY LIPNILAALV FLLPPLRRHM ERSNWRIIRL LLWWSQPKLF
VGRGMHEDMF SLFKYTLFWI LLLISKLAFS YYVEILPLIG PTKLIMDLRV GNYEWHEFFP
NVKHNIGVII SIWAPIVLVY FMDAQIWYAI FSTICGGING AFNHLGEIRT LGMLRSRFDA
VPIAFSARLV PSSKEESKKH HLVILLLSIV QQQDETWERK NIAKFSQVWN EFINCLRMED
LISNRERDLL LVPYSSGDVS VVQWPPFLLA SKIPIALDMA KDYKRKDDAY LFKKIKNDAY
MNSAVIECYE TLRDILYGLL DDEDDKFYIN TSFNTTLQIL MTTYAINFFP SVFLFCRIME
SYQHRKDHHT ERKEEKFQKL NLNLMRNRSW MEKVVRLHLL LTVKESAINV PMNLEARRRI
TFFTNSLFMN MPSAPKVRNM LSFSVLTPYY KEDVLYSEEE LNKENEDGIS ILFYLQKIYP
DEWNNFWERI NDPKTVNPAK EKMDLVRQWV SYRGQTLFRT VRGMMYYRQA LELQCFLDMA
EDPAIFGGYR IGVDSLNYQD QMTSAARSLA VADMKFTYVV SCQVYGAQKK SSEARDRSCY
QNILNLMLMY PSLRIAYIDE REETVNGKSE KVYYSVLVKG GDKLDEEIYR IKLPGPPTDI
GEGKPENQNH AIIFTRGEAL QTIDMNQDNY LEEAFKMRNV LEELLKSRRA DRKPTILGLR
EHIFTGSVSS LAWFMSNQET SFVTIGQRML AYPLRVRFHY GHPDIFDRLF HITRGGISKA
SKTINLSEDI FSGFNSTLRG GYVTHHEYIQ VGKGRDVGMN QISQFEAKVA NGNGEQTLSR
DVYRLGRRFD FYRMLSFYFT TVGFYFSSMV TVLTVYVFLY GRLYLVLSGL EKAILEDPSI
RQNKSLETAL ATQSVFQLGL ILVLPMVMEI GLERGFRTAI VDFIVMQLQL ASVFFTFQLG
TKAHYYGRTI LHGGAKYRAT GRGFVVFHAK FADNYRFYSR SHFVKGLELM VLLVVYEAYG
RSYRSSNLYL FVTFSMWFLV ASWLFAPSVF NPSGFEWQKT VDDWTDWKRW MGNRGGIGIQ
PDRSWESWWD AEQDHLKHTD IRGRVLEIIL ACRFFIYQYG IVYHLNIAHH SKSILLVVAS
FSTLVSNAAC IFYLLHAQMV SMGRRKFGTD FQLMFRILKG LLFLGLVSVM TVLFVVCGLT
IADVFAGMLG FLPTGWAILL IGQACRPLLK HIGFWESIKE LARAYEYVMG MIIFMPVVIL
SWFPFVSEFQ TRLLFNQAFS RGLQISMILA GRKDRTATS
//
