ID A0A445IAN0_GLYSO Unreviewed; 2006 AA.
AC A0A445IAN0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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};
DE Flags: Fragment;
GN ORFNames=D0Y65_031832 {ECO:0000313|EMBL:RZB82928.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:RZB82928.1, ECO:0000313|Proteomes:UP000289340};
RN [1] {ECO:0000313|EMBL:RZB82928.1, ECO:0000313|Proteomes:UP000289340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB82928.1};
RA Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT "A high-quality reference genome of wild soybean provides a powerful tool
RT to mine soybean genomes.";
RL Submitted (SEP-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:RZB82928.1}.
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DR EMBL; QZWG01000011; RZB82928.1; -; Genomic_DNA.
DR Proteomes; UP000289340; Chromosome 11.
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:SF22; CALLOSE SYNTHASE 8-RELATED; 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 ECO:0000313|EMBL:RZB82928.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000289340};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RZB82928.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 561..580
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 600..624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..657
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 677..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 739..760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 813..832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1572..1594
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1630..1647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1659..1676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1745..1764
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1848..1865
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1885..1905
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1912..1933
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1953..1974
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 372..488
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 505..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RZB82928.1"
SQ SEQUENCE 2006 AA; 231851 MW; EE467C489F769B5B CRC64;
STKQSAPKVT SLSKHYGEDS TYIPCIHVIT LLLVSYLTAM SEIVPAEPIG GIYFERGETS
TASASASASE TPHVTLAITN GSNNVEYVPE PFDSERLPTV FASEIQRFLR VANLLGKEEP
RVAYLCRVHA FVIAHNLDKN SSGRGVRQFK TSLLHRLEQD EHVTKKKGTS DIRELKNVYR
AYRDYYIRHE KAFDLEQSRR ERLINARDIA TVMFEVLKTV TDPASSQALI QGNAIHKKTE
FSILPLEQGC IQHAIMQKSE IKAAIAVIRN VRGLPPVQDF KKDGAFVDLF DFLQHCFGFQ
EANVANQREH LILLLANMQT RQTHNQTSVL KLGEGGVDEL MRKFFKNYTN WCKFLERKSN
IRLPLVKQEA QQYKILYIGL YLLIWGETAN LRFMPECLCY IFHHMAYELH GILSGAISLT
TWEKVMPAYG GETESFLNNV VTPIYTVIRQ EVANSKGGAA DYSVWRNYDD LNEYFWSPDC
FKIGWPMRLD HDFFFVKPRN KPEPDVKNAL VVSPGKTKEK KKREKRDEEE PEDTREEIHE
QQWLGKTNFV EIRSFWQIFR CFDRMWSFFI LSLQAIIIIA CHDLGSPLQL LDAVVFEDII
TIFITSAYLK LIQAILDVAF MWKARYTMES SQKVKLVVKL VLATIWTIVL PVCYANSRRK
YTCYSTKYGS LVEEWCFTSY MVAAAIYLTT NAVEVLLFFV PAVAKYIEVS NYKICKVLSW
WTQPRIYVGR GMQEDQVSVF KYTLFWILVL SCKFVFSYSF EIKPLIAPTR QIMKIGVKKY
EWHELFPKVK SNAGAIVAVW SPVVIVYFMD TQIWYSVFCT IIGGLYGVLH HLGEIRTLGM
LRSKFDSLPS AFNVCLIPPS SKRGKKKRKG LLSNIFQKLP DEKNATAKFV VVWNQIVNHL
RLEDLISNRE MDLMMMPVSS ELFSAKVRWP VFLLANKFST ALTIAKDFEG KEEILVKKIT
KDKYMFYAVR ECYQSLKYVL EILVVGSIEK RIICDILSKI EKHIQETSLL KNFNLKVLPA
LHAKVVELAE LLMEGDKDHQ HKVVKALLDV FELVTNEMMF DSRILDMFHF PEQNECGFVY
FRNDDQLFDS VEMNRDFYPF AKENSIHFPL PESGPLMEKI KRFHLLLTVK DTAMDVPSNL
DARRRISFFA TSLFTDMPDA PKVHNMMPFC VITPHYIEDI NFSLKELGSD KEEDSIIFYM
QKIYPDEWTN FLERMGCDNR KSLEDEHKTE DLRLWASFRG QTLSRTVRGM MYYREALKLQ
AFLDMAEEED ILEGYETAER GNRALFARLE ALADMKYTYV ISCQSFASQK ASNDPRYQDM
IDLMIRYPSL RVAYVEEKEE IVQGKPHKVY SSKLVKVVNG YEQTIYQIKL PGPPHLGEGK
PENQNNAIIF TRGEALQTID MNQDNYLEEA LKMRNLLQEF LRRQGRRPPT ILGLREHIFT
GSVSSLAGFM SYQETSFVTI GQRVLANPLR VRFHYGHPDV FDRVFHITRG GISKASKTIN
LSEDVFAGFN STLRRGCISY HEYLQIGKGR DVALNQISKF EAKVANGNCE QTISRDMFRL
GRQFDFFRML SCYFTTVGFY FSSLISVIGI YVFLYGQLYL VLSGLERALI IEARIKNVQS
LETALASQSF IQLGLLTGLP MVMEIGLERG FLTALKDFVL MQLQLAAVFF TFALGTKTHY
YGRTLLHGGA KYRPTGRKVV FHASFTENYR LYSRSHFVKA FELLLLLIVY NMFRRSYQSS
MAYVLITYAI WFMSLTWLCA PFLFNPAGFS WTKTVDDWKE WNKWIRQQGG IGIQQDRSWH
SWWHDEQAHL RWSGFGSRLT EVLLSLRFFI YQYGLVYHLD ISQHSKNFLV YVLSWIVIVA
IFLLVKAVNM GRQLLSANYQ LGFRFFKAFL FLAVLAIIFT LSVICELSLT DIFVCCLAFM
PTAWGLIMIA QAARPKIEHT GLWDFTRALA REFDYGMGIV LFGPIAILAW LPIIKAFHAR
FLFNEAFKRH LQIQPILSGK KKKHRT
//
