ID A0A9D5HRM9_9LILI Unreviewed; 2380 AA.
AC A0A9D5HRM9;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
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=J5N97_004352 {ECO:0000313|EMBL:KAJ0985996.1};
OS Dioscorea zingiberensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Dioscoreales; Dioscoreaceae;
OC Dioscorea.
OX NCBI_TaxID=325984 {ECO:0000313|EMBL:KAJ0985996.1, ECO:0000313|Proteomes:UP001085076};
RN [1] {ECO:0000313|EMBL:KAJ0985996.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Dzin_1.0 {ECO:0000313|EMBL:KAJ0985996.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAJ0985996.1};
RA Li Z., Yang C.;
RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAJ0985996.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Dzin_1.0 {ECO:0000313|EMBL:KAJ0985996.1};
RX PubMed=36204203;
RA Li Y., Tan C., Li Z., Guo J., Li S., Chen X., Wang C., Dai X., Yang H.,
RA Song W., Hou L., Xu J., Tong Z., Xu A., Yuan X., Wang W., Yang Q., Chen L.,
RA Sun Z., Wang K., Pan B., Chen J., Bao Y., Liu F., Qi X., Gang D.R., Wen J.,
RA Li J.;
RT "The genome of Dioscorea zingiberensis sheds light on the biosynthesis,
RT origin and evolution of the medicinally important diosgenin saponins.";
RL Hortic Res 9:0-0(2022).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + UDP + H(+); 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:ARBA00047777};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:KAJ0985996.1}.
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DR EMBL; JAGGNH010000001; KAJ0985996.1; -; Genomic_DNA.
DR OrthoDB; 1880850at2759; -.
DR Proteomes; UP001085076; Miscellaneous, Linkage group lg01.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR058851; CALS1_helical.
DR InterPro; IPR010820; DUF1421.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48_dom.
DR PANTHER; PTHR12741:SF7; CALLOSE SYNTHASE 12; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF25968; CALS1; 1.
DR Pfam; PF07223; DUF1421; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP001085076};
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 832..851
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 863..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 904..925
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..969
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1026
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1055..1072
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1863..1885
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2034..2056
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2140..2161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2173..2194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2201..2225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2237..2257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 681..796
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 27..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 116..150
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 38..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..329
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2380 AA; 273320 MW; 271DA85496FB7598 CRC64;
MASGSSSSRA GSGGRTFDFG SDDVLCSYDD FGPQDPPNGR RSDPSAKDLH ESRMGRSSVN
FHDQENLSKD DVISAVEKCM KKYADNLLRF LEGISGRLSQ LEVYCYKLER SIGEFRTDLT
RDQSEADQKL KSLEKHLQEV HRSVQILRDK QELAETQKEL AKLHFVRKES SSPSLSKRNE
EGTAPSVSEA KKHDEADNIP NQHLALALPH QVAPASLPIR TSEQSPYKEP SLQQPAGAPL
NMQQDRYVLN QPGTFYPPQM QPEYQYIQPR PQIQDPSAQV PQQQSQIISQ PQPNSLPQYQ
PQWTQQPSQH APQQIIQQPP SSQAQIRSQT PSSYPPYLPN QPAIPMPQTF PRGSGSSVSQ
PPHQAHIQRQ PQPETNQSSF QQNLNKVGYM GATPQYTQVT PQNQQNQSYN PMYSLDGSRG
PQIFQTPNAN YPPANMPAPH NQQLPPSSSS FHHPGAQLIR SHPLGEMIEK AVNMGYSRDH
VLSVIHHDDA TCKVPTVLKQ RANVHRDRRS GPRSDAMMGR QKRQGPPQDE RRGGGGAAMA
AAEEEPYNII PIHNLLAEHP ALRFPEVRAA MAALLAVGEL RTPPFIRWHD GLDLLDWLGA
FFGFQRDNVR NQREHLVLLL ANAQMRLQPP PDNIDTLDPA VVRRLRRKLL HNYTAWCAYL
GRKSNVWVSD SPSRRYPDAP RRDLLYSALY LLVWGEAANL RFLPECLSYI FHFMAMDLNR
ILEGYNDDNG RPALPAVSGD GAYLTRVVTP LYKVIKAEVD SSRNGTAPHS AWRNYDDINE
YFWSRRCFDR LRWPLDLSTN FFAPPPNRNR VRKTGFVEQR SFWTIYRSFD RLWVMLILFL
QAATIVAWEG NEFPWQGLRS RDVQVRALTV FITWAAIRFL QSILDAGTQY SLVSRETPWL
GVRMVLKSIV ATGWAVAFGI LYARVWDQRN HDRRWSPAAN QRLVDYLMAA GVFILPELLA
LALFILPWIR NFLEKTNWRI LYALTWWFQT RTFVGRGLRE GLIDNIKYAL FWVVLLAVKF
TFSYFLQIKP MVRPSKDIFN LNNVQYQWHE FFTRTNRFAV VLLWIPVVLI YLMDIQIWYA
IFSSLVGALV GLFSHLGEIR NVEQLKLRFQ FFASAMQFNL FPEEQLFKDR GTLKSKFKDA
ILRLKLRYGF GRPFKKIESN QVEANRFALI WNEIITTFRE EDIISDHEVE LLELPPNSWN
IRVIRWPCFL LSNELLLALG QAKELVAPDK KHWRKICKNE YRRCAVVEAY DSVKHLLLEI
VKDNTEEHSI ITHIFYGIDD AIRAGRLTEE YKMTVLESIH SKLIVLLKIL TDAKKDMNKV
VNTLQTLYDL AIRDFPTDKK KIEQLREAGL VPSRPIGTGL LFENAIELPP ADNSIFYRQV
RRLYTILTSR DSMNNVPKNL EARRRIAFFS NSLFMNMPRA PQVEKMLAFS VLTPYYNEDV
IYSKDNLKNE NEDGVSTIFY LQKIYEDEWM NFLERMQREG VVNEDEIWSG ERLRDLRLWA
SYRGQTLSRT VRGMMYYYKA LKMLTFLDSA SEVDIREGSR ELATFGDSMR HDNVVDGVEN
RYPSSRNLSR ASSGVSLLFK GHESGTALMK FTYVVACQIY GTQRGKPEGE EILYLMKNNE
ALRVAYADEV RTGRDEVEYY SVLVKYDQQL QKEVEIYRVK LPGPLKLGEG KPENQNHALI
FTRGDAVQTI DMNQDNYFEE AVKMRNLLEE YSHTYGARKP TLLGVREHVF TGSVSSLAWF
MSAQETSFVT LGQRVLANPL KVRMHYGHPD VFDRLWFMTR GGISKASRVI NISEDIFAGF
NCTLRGGNVT HHEYIQVGKG RDVGLNQISM FEAKVAGGNG EQVLSRDVYR LGHRLDFFRM
LSFFYTTVGF YFNTMMVVLT VYSFVWGRLY LALSGLEDSI KQRANSTNNT ALGTVLNQQF
LIQLGIFTAL PMIVENSLEH GFLPAVWDFL TMQLQLASMF YTFSMGTKSH YFGRTILHGG
AKYRPTGRGF VVQHKSFAEN YRLYARSHFI KAIELGVILT VYASYSAISK DTVVYIVMTI
SSWFLVVSWI MAPFAFNPSG FDWLKTVYDF EDFMNWIWYR GGVFTKADES WETWWYEEQA
HLRTTGLWGK LLEIVLDLRF FFFQYGIVYQ LYIADKSTSI AVYLLSWIYV VVAAGIFVLM
GYARDKYAAK EHIYYRAVQS FVIILVILVI IILLKFTNFK LIDIFTSLLA FIPTGWGLIS
IAQVIRPFIE STVVWDTVVA VARLYDILFG VLLAVAFRYP GLLLAKNLIL TSEVQSSTTE
CRVLKCKAGG GSVAEPTPNY CQMMQRVHHI YHPQKLDKTH MHSSIKGSSN SMVGRCSLHL
PVSLPLRFWK AANKEAKRER RASISCVFKL LLEGRLLIQP
//
