ID A0A314YXG8_PRUYE Unreviewed; 1308 AA.
AC A0A314YXG8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=Pyn_36795 {ECO:0000313|EMBL:PQQ12885.1};
OS Prunus yedoensis var. nudiflora.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=2094558 {ECO:0000313|EMBL:PQQ12885.1, ECO:0000313|Proteomes:UP000250321};
RN [1] {ECO:0000313|EMBL:PQQ12885.1, ECO:0000313|Proteomes:UP000250321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jeju island {ECO:0000313|Proteomes:UP000250321};
RC TISSUE=Leaf {ECO:0000313|EMBL:PQQ12885.1};
RA Baek S., Kim J.-H., Choi K., Kim G.-B., Cho A., Jang H., Shin C.-H.,
RA Yu H.-J., Mun J.-H.;
RT "Draft genome of wild Prunus yedoensis var. nudiflora.";
RL Submitted (FEB-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}.
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:PQQ12885.1}.
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DR EMBL; PJQY01000330; PQQ12885.1; -; Genomic_DNA.
DR STRING; 2094558.A0A314YXG8; -.
DR Proteomes; UP000250321; 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; IPR023175; Vta1/CALS_N_sf.
DR PANTHER; PTHR12741:SF47; CALLOSE SYNTHASE 9; 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 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:UP000250321};
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 45..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 573..592
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 675..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 740..761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 800..827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 418..530
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1308 AA; 150827 MW; A808AD51CB41E730 CRC64;
MKGMTSWIGE NRFYAEPFKK SSSPQSSGVT PYGGMRWLGP AKHTSARLVL ICVGLLGLAL
IADFLWASSP RFLYALISQI GKMSRVEERW EHLVRAVLSR ERMGTDAYGR HSTGIAGNVP
SSLANNRDID EILRAADEIQ DEDPNISRIL CEHAYSLAQN LDPNSEGRGV LQFKTGLMSV
IKQKLAKREG GTIDRSQDIA RLQEFYKLYR QKNNVEKLRE EEMKLRESGA FSGNLGELEK
KTVKRKRVFA TLRVLGTVLG QLTEEIPEEL KRVMESDAAM TEDLIAYNII PLDAPSITNV
IVSFPEVQAA VSALKYFRGL PNLPTDFSIP ATRDPDMLDF LHYIFGFQKD NVSNQREHIV
LLLANEQSRL RIPEETEPKL DEAAVRNVFL KSLENYIKWC DYLCIQPIWS NLEAVSTEKK
LLYISVYFLV WGEAANVRFL PECLCYIFHH MAREMDEILR QQIAQPANSC SSENGVSFLD
QVIYPLYEVV AAEAANNDNG RAPHSAWRNY EDFNEYFWSL HCFELSWPWR KGSSFFERPI
RGSKNILKSG RSQHRGKTSF VEHRTFLHLY HSFHRLWIFL VMMFQGLTII AFNKGQLNAK
CIREVLSLGP TFVVMKFLES VLDILMMYGA YSTTRRLAVS RIFLRFLWFS TASVVISFLY
VKALQEESKQ NGNRVIFRLY QIVIGVYAGI QFFISVFMRI PACHSLTNQC DRWPLIRFVK
WMRQERHYVG RGMYERTTDF IKYMLFWLVI LSVKFAFAYF LQIKPLVKPT KTIVTLGPIR
YSWHDLVSKN NHNALTVASL WAPVICIYLL DLHVFYTLIS GVWGFLLGAR DRLGEIRSLE
ALHQLFEQFP RAFMGTLHVP LPNRTSEQAS SEVMEKNKVD AGRFSPFWNE IIRNLREEDY
ITNLEMELLA MPKNSGKLPM VQWPLFLLSS KIFVAKDIAV ESRDSQDELL ERISRDDYMK
YAVQECFLTL KLILSEILEG EGSMWIEQVY KDIHESIAKK SIHVDFQLNK LPLVISRVTA
LMGILKEGGT SELEKGAVKA VQDLYDVVHH DVLSVNMRGN YETWKLLSNA RTEGRLFAKL
KWPKDPELRA QVKRLHSLLT IKDSAANIPK NLEARRRLEF FTNSLFMEMP EPKPVREMLS
FSVFTPYYAE IVLYSMAELQ KKNEDGISIL FYLQKIYPDE WKNFLARIGR DENALDSELF
DNATDILELR FWASYRGQTL ARTVRGMMYY RKAFMLQTYL ERLNSAVSDV EAAISSNDTA
DTRAFELSPE ARAQADLKFT YVVTCQIYGK QKEGQKPEAA DIALLMQR
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