ID A0A371DVV3_9APHY Unreviewed; 2350 AA.
AC A0A371DVV3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=OH76DRAFT_1395807 {ECO:0000313|EMBL:RDX56682.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX56682.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX56682.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX56682.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
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; KZ857380; RDX56682.1; -; Genomic_DNA.
DR STRING; 139420.A0A371DVV3; -.
DR Proteomes; UP000256964; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11323; AmyAc_AGS; 1.
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; 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 Hydrolase {ECO:0000313|EMBL:RDX56682.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000256964};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RDX56682.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..2350
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016720322"
FT TRANSMEM 1058..1084
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1928..1948
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1960..1979
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1986..2005
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2025..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..2110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2170..2194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2274..2292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2322..2341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..522
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1628..1744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1868..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1643..1702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1719..1743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2350 AA; 263300 MW; 99474DC64A9B241F CRC64;
MWVRTAIVSL LALAQWGVAS PYRDDLVDYN LNTNKNAQSP LQYSTDKRPS YTKSPDNWRS
IPFYTILLDK FADGDPSNND YFGTMYEWDW RETQLRFGGD LKGLVSKLDY LQGMGIKGIF
ISGTPFINML WQADSYSPLD FTVLDPHWGT LADWQATIDA IHARGMYIMA DFTVGTMADL
VGFKGYLNTS TPFDLGEYDA VWKDPLYAPW GFNEYKDFSI DNGYNESCQL PTFWADNGVI
QDIDWKSGCK LSDFDQYGDM EAFGVHPDWQ RQLSKFASVQ DRLREWKPEV LQKLQTFSCM
AITALDIDAI RIDKSTQVTV DALASWASST RACAANLGKT NFYIPGEVTG GDYFGSIYYG
RGRTPTQRPP GFLQAANLSA DMDQYFLRDK PLNALDGAAF HYSTYRSLAR FLGMDGNLQV
AFDVNSNFVT AWNEMFVNND FLNPHSGDVD PRHMFGTSNF DVFRWPSLEN GNQRSALGTF
ITNLVMPGVA LYYYGEEQNF YLYDTTASNY LYGRQAMMSN KAWQRHGCYA LGSDQYFNMP
LGKAILGCED DWNSLDHFDP TTDSRRLFAQ FLYLRSHFAS LQDGFNLVQR GNWTYNIARP
GSNGTLTEMG LWSVSRAPID NVQKLTGNTN QVWMLYSNEN QTKTWSYDCK GDLWISSPFE
SGNVVRNLFY PYENYTLQDS GSPYFNDGKA PWYGCLDTVT MEPYSFKALV PIDQWVPPSP
MLTKFTPGHD ARLQAEPGDV NATSVDIVLE FSAPMDCTSV TSAISFTMSG SGDAPTINQN
SIKCLTLTNV DPPKIPGTPV SQWSWSATLQ NFPDGILDIA IKNAVTQTGV STNVTDHLLL
RKGSANNVMV FPESDYNSTA FGVSDGTYKF THSAWGADMF RYSANFGKNW TDWQKYEPVS
TFDPKLFEDS DNFWEGHHVM VQYWSDLAKA ATVVVHADNG YSHPRRVPQL LARGPFNQWG
FDKGITAQMT QNDNGKWELE IMASWPTYVQ LNVFGYDNYY YGDIDGDGVL DRLPPNTAAP
NYLNISAPPK PHLAWALVVD DSTLTWTLEP RGESIIGAIT YALLLSVPLI TGALAVAIFM
WSFYGIRYNK WGVKPNKDHS SYFPILGSLG NKSSTNVKDH TPMSEKVFGH HHKQHEIIGW
PEDKNKRRCV LIATLEYEII DWKLKVKIGG LGVMSSLMGK AMTDVDLIWV IPKVKDLEYP
PGEPADPIEV IIFGEPYLIE VETHVLDNIT YVILDSPVFR AQTKADPYPA RMDDLSSAIF
YSTWNQAIAA TVRRYPQIDI YHVNDYHGAL APIYLLPKVL PVCLSLHNAE FQGLWPLRTK
EEMKEVCSAF NISKEHCTKY VQFGNTFNLL HAAASFISVH QKSIGVAGVS DKYGKRSWAR
YPALWTLKHV DSLPNPDPTD IAALDENPIS VRDIQIDQGA EAERPEHKRQ AQEWAGLKQD
PNADLFVFVG RWSKQKGVDL IADVMPSLLE KKPSIQLITV GPVIDLYGRF AAEKLARLME
LYPDRVYSKP EFTALPPYLF SGADFALIPS RDEPFGLVAV EFGRKGALGV GSRLGGLGLM
PGWWFPVEST STEHMMSQLT KTIKMALKST EEERALLRAR SAVQRFPVVE WRQRMEDFHK
RSIGASRSLA GPNAWRPSDA AFNPDTYRSQ QEPSSWEPEY QAYPSQPEWD SRSIAESQSP
QILTPGTPGS PGQWSQETLT PGGDPHLSAP RLLPQGRRGS VSTDISDNEG DYFSSQPSPG
ETRQEFGNFL ERANRTIARD QKAVPDPFLD AAPTRPFGAH SRASSVESIA SIVDEKQNSP
LNKAIASFTD ADGGVASEFV QKLQMLNAHN SKHELSIEKY LMKSEEAFFD KVKKDKLSSA
ASVRSSQRDS VWGTPAPSSF DHSRPSSPSG HSFAPSINGD YSGPLPNGQD VVIMTGLQIA
LSREVFGWPL YTIIIALGQM LAATSFQITL LSGQNSETNL QLYVLGGVFL ASSIVWYFLF
RVKPSVYVLS IPWVFFGIAF FLIGLPSVTS SLNVAHVALS SAATWSYAIA SAAAFCFFGL
NFGEEAGAAT EVWMLRACIV QGSQQVWVAA LWYWGYMLDG VEQNNMAPWW IVLIVWPLAV
MSFLFAYLML FGLPDYYRQT PPKVPNFLRT LFRRKIVLWF LGSEILRDYW LSGPYGRNWG
FLWNVPITKW QIALLVVAFF VVVWGMMMGI LTWLSKTHTW LLPVFAVGLG APRWCQMLWG
TSSLALYIPW AGHAGPYLGV CLWLWLGVLD AIQGVGLGLI LLQTLSRLHV CATLAFAQVI
GSICVMVARA TAPNRIGPES VFPDAAQWDF DDGLKGSPLA SAPFWVALIC QLIIVIGYFW
FYRKEQLARP
//
