ID A0A0K6GEM4_9AGAM Unreviewed; 2349 AA.
AC A0A0K6GEM4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=RSOLAG22IIIB_06398 {ECO:0000313|EMBL:CUA76935.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA76935.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA76935.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA76935.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19749, Rhea:RHEA-
CC COMP:11150, Rhea:RHEA-COMP:11151, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28100, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC EC=2.4.1.183; Evidence={ECO:0000256|ARBA:ARBA00000687};
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000256|ARBA:ARBA00006122}.
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DR EMBL; CYGV01001734; CUA76935.1; -; Genomic_DNA.
DR Proteomes; UP000044841; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0047657; F:alpha-1,3-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR InterPro; IPR013534; Starch_synth_cat_dom.
DR PANTHER; PTHR47182; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE AGS1-RELATED; 1.
DR PANTHER; PTHR47182:SF2; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE MOK13; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Maltose metabolism {ECO:0000256|ARBA:ARBA00026248};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000044841};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..2349
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005503057"
FT TRANSMEM 1065..1086
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1927..1947
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1959..1978
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1985..2004
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2024..2042
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2054..2075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2087..2109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2130..2149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2169..2191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2203..2229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2241..2261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2273..2291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2321..2340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..524
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1636..1743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1856..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1704..1718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1856..1875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2349 AA; 263526 MW; 9354E69ED89B3648 CRC64;
MRLPSPGPLG LAVLALLSGT LGMPYNESLT DYNMNINQNA QTVLEYDSTR PNKTYTPSPT
NWRDYPIYTI LLDKFADGEP GNNDYFKTMF ENDWREVNLR FGGDVRGLMR RLDYIQGMGV
GCIFIAGTPF LNMPWQADSY SPIDFSVLDP HWGNIDDWRA LTDAIHARGM YLMLDFTVGT
MGDMIGFEGH LNTSTPFSIN EYNAVWKKPR YTPWGIEEYP DFKIKNTIND TCKLPTMWND
AGEIVPIDKT GCYASEFDQY GDMEAFGVHP DWNRQLSKFA SVQDRLREWN VDVRAKIQVF
SCLAIKALDI DAIRIDKATQ VTVDALADWS AHTRQCAKEM GKSNFFIVGE VTGGDTFGAL
YLGRGRTPTQ RPTSFEAGAN LTSSQNQYFL RDSNRHSLDS VAFHYSVYRA LSRILGMDGN
LQVAYDTIAN FFDVWTTMGK SNDFLNAETG EFDPRHMYGI SNFDVFRWPS IVNGTQKQML
GTFINSLLMP GIPLIYYGEE QDFYLFDNGA SNYLFGRQPM TSSQAWQRHG CYKLGSEQYF
NMRLEKSLLG CEDDWNSLDH FDPSAGSRRM MAHFHYLRKQ YPVLTDGFRL LQNGNWTSYI
QLPGSNKTET EIGWWSVSRS PLASQSNFNS TVRDIWMIFT NMNVTESYTY DCNSALWVST
PWVGGTTIRN LFYPFETYTL QDSQSSFNNN GQAPWVGCLP SVTLQPYSYK AFVPVANWVA
PPPMLTRFSP GHDVRLHAES GDTNATTVDI VLEFTTEMSC TSVTNGLSFN VSSSGHGSTP
TINTGSVQCG NITNPIQPTL PGDTPSAWSW SGTLNNVPDG IIEIRVNNVA AADGQRTTGS
TDHFLLRKGS SKNVMVFPDA DYDNEAFGYS DGSYTFTHSA IGADRFRYSW NYGKNWTDWT
AYEDKTTIPG SVFNPTDDMF WEGEHLIVQY WSELAGSSTA VVHADRGFSN PRRVPQFIAR
GPFNTWGFDK GISAQMVQNE KGLWELPIMA TWPSYVQLNV FGYDDYFYGD TNGDGVMDRL
PPNSATPNYL NMSAPPKPYL SWALFVDDKT QRWYLEPRGN SAVGAIMYAL LLSIPMITAV
IAVVIFRRNF YQIRINQWGT APKADASYFP ILGALGIMKA NQHSDDKGGI PGTPVVEKGL
HGNKAYTGPV IGWPENPNKR RQVLISTLEY EIIDWKLKVK IGGLGVMSSL MGKSMTDCDI
YWVVPKVKDL EYPAGDPADP IEVIIFGEPY LIEVEYHVLD NITYIILDSP VFRAQTKADP
YPARMDDLSS AIFYSTWNQA IAETVRRFPV IDIYHINDYH GALAPLYLLP RVLPVCLSLH
NAEFQGLWPL RTKEEMKEVC SAFNLSKEVC TKYVQFGNTF NLLHAAASFI SVHQKSVGVA
GVSDKYGKRS WARYPALWTL KHVDSLPNPD PSDIAALDEK PVDMANVAID QTAEAQRPEH
KRQAQEWAKI KQDPKADLFV FVGRWSKQKG VDVIADAMPS LLEKRPSIQL IAVGPVIDLY
GRFAAEKLAR LMEMYPDRVF SKPEFTALPP FLFSGADFAL IPSRDEPFGL VAVEFGRKGA
LGVGSRLGGL GLMPGWWFPV ESTSTNHMLS QFTKTIKLAL KSTEEERAML RARSAVQRFP
VVEWRQRTED FHRRSINTSR RLAGPDAWSE KDCIKPGQSG NRAIQGMDTE DWNPLHKPEP
TQPNWDAQST RSGISVGDTL HAPRAGHQTN SSRASFQSEA SDYEDHSRAP SPTSTRPDDF
GGFLNRANKA IAREHKHVAD PFIDDNAAPN RPFGMHSRVS SVESISSIMD EKGASSPLNK
AMASFTDADG EVAQAFVAKL QLLTPENSSK ELSIEKFLTK SEEAFFDKVK QDKINSSAAS
IRSRRDSSWG TPSHFDSRPA SPAFPQTPGT PGEGFDTKNY SGPLPNENDT PNMTALQISM
QRTFYGWPLY TIIIAIGQML GATSFQITLL SGQNWQTNLQ LYVLGGIFLA ASVVWWALFR
LKPSVYVLSA PWIFFFLAFF IIGIPALSDS LTPYRQAFGS AATWAYAVAS AAAFLFFGLN
FGEEAGAATE VWTMRACIVQ GSQQIWVAAL WYWGYRLNGS DPNVKPPWWT ICILWPLAFI
SLFFGYCLMW GLPEYYRQVP PKVPNFAKTL FRRHIVVWFL ASEILRDYWL SGPYGRNWSF
LWNSPIPKWA ILLLIIAFFI GVWFIMMYIL TRITKTHTWF LPIFAVGLGA PRWCQMLWGT
SSLALYIPWA GRAGPYLGTS LWLWLGVLDA IQGVGLGMIL LQTLSRLHVC ATLALAQVIG
SVCVMVARAT APNRIGPGSV FPDAAKWDFS DGLKGSPMAS APFWVALVSQ LVIVFGYFWF
YRKEQLARP
//
