ID A0A2J6SIA9_9HELO Unreviewed; 2236 AA.
AC A0A2J6SIA9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=K444DRAFT_657437 {ECO:0000313|EMBL:PMD50489.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD50489.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD50489.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD50489.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) 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; KZ613913; PMD50489.1; -; Genomic_DNA.
DR STRING; 1095630.A0A2J6SIA9; -.
DR InParanoid; A0A2J6SIA9; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000235371; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000235371};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PMD50489.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..2236
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014461024"
FT TRANSMEM 1841..1862
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1882..1899
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1906..1929
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1941..1961
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1973..1994
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2014..2032
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2052..2072
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2092..2114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2126..2145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2157..2177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2184..2203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..493
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1629..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2236 AA; 251440 MW; EAA46EEF3C43640B CRC64;
MISLIIILIS FAFNFVSSLK FDYQEIEYNL NENKTASNPL EYWGEWPNHS YQPSPSNWRF
PFYTLFLDRF VNGDPSNDDI NGTVFEHDVM SNQFRHGGDI AGLGIYIAGS PFVNLPWKAD
SYSRAAVTEI HSRGMYVILD NTMSTMGDLI GFKGFENASA PFSPTEYQVE WKSDRHYLDF
DFGNTYNAIC QYPRFWDESG FPVTKSTDPN VAQLRGCYDS EFDQYGDVGA FVAVPIWHRQ
LCTFSSVQDR LREWVPSVRQ KIEHFSCLLI TMLDIDGFRI DKGAQVTVDA LADSGEFIRQ
CARRFGKTNF FISGEITFGD TLGSVYLGRG RQPDQVPDNP GQAVSAANFS DSSFFLRNKD
KNAFDAAAFH YSIYRSLTIF LGMEGNLTIA YDVPTNFVDA WNIMLATNDL VNANTGEFDP
RHMYGVTNQD VFRWPAIKDG TKKMLLGLFI TTLHMPGIPL LLWGEEQAFY VLDSTADNYI
YGRQAMSSSP AWQIHGCYGL GSFQYYNFSV DSALHGCHDD SVSLDHRDPA HPIRNIIKSM
YHARLSNRYP VLNDGYLLQS LSNQSRDIFL PGSSGAATEI GIWSVMRYQY PNLQKLDESG
ESQPIWLVYQ NDDHRVKYSF NCSSNETAFI APFPQGTVVK NILAPHDEFE LEAGPRKLGI
DGSEEFNGCA AELELDAYGF KAYVPKDRWV APLPMVTNFL PGHDTRILST VRPNETETVD
IELHFSEIMD CNHITSNLLI SSTTINNISA QLDQNKISCA VLPTPDIPLY VGGIPSTWAW
KATLLNVSNG IQSITVQNAT TLRHQSFTNS KDRFLFRIGQ ENNPMVFPPL ANYSREILFR
NQSSEDLYVS HKAAGADKFR YSLNWASSWS AWEDYGGGNT TLVPQPWSGT KRQYWDGEHV
TLQYWSRLTG SSDHVQHADL SSMEKTYSQP RRYPHLFAEG PFNKFGFDQG LKNDFYLDPH
DSIWKFYLMA EWPSTLQVNV WGTNPDGQLD QTMVFGDIDN DGVLDRMLPD SLGEAMINFA
SPPTPYLAFR LEVNDGTLGF RRVPVGSHRT QIFVYVLLWT IPVSTGMVSV WIYMSAFYSV
KLNESGVDQK EGITLFRHRI DSEKLAQKYL GAPNKVLSAA SRFQSYLRST VGPPVPTMTE
AGKQRTILIA TMEYGIEDWN IKIKIGGLGV WQTLVDQNLI WVVPCVGGID YPIDQKAEPM
HITILSNSFS VFVQYHKLRN ITYVLLDAPI FRQQDNTGDL NSAIYYSTWN ACIAETIKRF
PIDLYHINDY HGAAAPLYLL PQKLPVVLSL HNADFQVEIS KVFNLDMAVI QKYIQFGESF
NLLHSASSYL RVYQGGLGAV GVSSKYGKRS YTRYPIFWGL KQIGRLPNPD PSDTEPWNPT
EAKQVIEVGP AFEFCRGVLR QKAQEWAGLD LDPTAELFVF IGRWSKQKGV DLIADVFPSV
LERHPRAQLI CIGPTVDLYG KFAALKLGEI MKIYPGRVYS KPEYTAVPPF IFMGAEFALI
PSRDEPFGLV AVEFGRKGAL GVGARVGGLG SLPGWWYTVE STTTKHLHQQ FKKSIEDAVA
SKTEMRAMMR AQSAIQRFPV AKWAEELDQI HSTVMRTSCG ERQLRLRLPS RFCAHPVVPT
VFSEVDFHRD RSGTRSSPSS LTANSRSRSR SNSAESSANG SPISGRPGRR VGATSLPPEG
HLQSPGTRTF SILSFDEAVG DRKDFNLQKT DPTFKDTDEK YYRAFQNMLH KLDGKTSEGR
LCIEKYLIES EMEWNKRRRE AKRDRGRASK ASSSDGSIYI ERRGSSLASL FGWTPAVESE
SSTSHEQISE SSTVVNETDE FMLDDDHDHE SFLKRWMVTK VLGWPIYSLL LVFGQIIAVN
SYQITLFTGS LADSGEETSE KLYILGTIYV ATSCMWWLMF RSFKSIFALS LPFFFYGLSF
LLIGILASLP GGVRRDWMAR AATGVYVTAS SSGSLFTALN FGAEGGATVK SWVYRASIIQ
GTQQILLAAL FYWARTASSS IRENANATST KLTAIALPIS ALLWFVGIAL SLSLPPYYRQ
RPGKIPAFYT ALLRRPITAW FFITVVMQNY FLSMPYGRNW TYLWSSKYAP TWTIVLLIVL
FFIILWMLAH PWIMPIFAIG LGAPRWAQML WGTSSFGLWL PWFVGGPVGG ALGGRAVWLW
LGILDSLQGV GLGMMLLQTL TRTHFAGTIM MAQILGTLVM MLAKATAPTR DGPGDVFPDF
SAGVGTSLHG NYWFWV
//
