ID A0A165GAJ8_EXIGL Unreviewed; 2340 AA.
AC A0A165GAJ8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=EXIGLDRAFT_740820 {ECO:0000313|EMBL:KZV90231.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV90231.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV90231.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV90231.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV426053; KZV90231.1; -; Genomic_DNA.
DR STRING; 1314781.A0A165GAJ8; -.
DR InParanoid; A0A165GAJ8; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000077266; 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; 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:KZV90231.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZV90231.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2340
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007858112"
FT TRANSMEM 1056..1081
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1908..1931
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1943..1962
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1969..1992
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2004..2025
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2037..2057
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2069..2092
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2154..2174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2256..2274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2304..2323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..515
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1620..1685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1671..1685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2340 AA; 263419 MW; B366117DDA26CDCC CRC64;
MLLVQLLLLA SARAMRYTDA LQDWNLNVNH SATSPLDYAP ATRQTYTPSP ENWRALPTYT
LLLDKFADGD PLNNDFFNTT FENDWNEVNF RFGGDVKGLR GRLDYLYGMG VRAIFIAGTP
FLNMPWQADS YSPIDFSILD PHWGTSADWR DLIDEIHRKN MYIILDFTVG TMADMLGFKG
HLNSSTPFSM MEYEAVWKKP PYAPWGIDEY QDFKFNNLRN ETCTLPTLWQ DDGTILDVVT
DTCYASEFDQ YGDMEAFGVH PDWQRQLAKF ASVQDRLREW DYHVRQKIKV FSCLAIRSLD
IDGIRIDKAT QVTVDALADW SMATRECATR VGKTNFFIPG EVTGGDTFGS LYIGRGRTPT
QRPPGFLAAG NVTRTQNQYF LREDKLAPLD SVAFHYSTYR ALCRFLGLDG NLQVAYDVDV
NFVTAWNQMF VNNDFLNPAT GEIDPRHMYG VTNFDVFRWP ALVNGTQRLM LGMFITSLVM
PGINLLYYGE EQDLHLLDSN AENYLYGRQA MSGTKAWQRH GCYQLGSEQY FNFPLERARL
GCEDDSSSLD HFDPTTPNRR LLTQFNYLRS TYPALQDGFN LVQWGNWTHR DELPGSNGTQ
TELGWWSVTR SALSTIQKFE DSPRSDQVWL LYTNENATHS YEFECDSKLW ISSPYTGGTK
VRNLFHPFEN YTLEDSRSSY YNDSKAPWRG CLPQLSLDAY SFKALVPADA WSPPPPMLTK
FEPGHDFRIR AEEGDSNATV VEIAFEFSVP MSCDGVTGGF SMQMFSSGVG GNPSLDQDSV
LCTTIENPRK PELPGLAPSA WRWTAKLRDV PDGILQLILT NVTTAEGAHT NIVDKVMLRK
GSLANVMVHP MSDYDNDALQ VMNGDFVFAH KAFGADLLRY TTNFGRSWSR WMDWEAATTI
PADAFRAQEN FWAGQHLTVQ YWSEVAGSSA HVVHADHNYG HERRVPQFLA RGPFNTWGYD
SGIPSVMQHV GDGRWELEIM ASWPTYLQLN VFGNDDYYYG DVDVDGVLDR LPPNSLALNY
VNLTAPPHPH LAWALIVDDY TGRWSLEPRG HSAIGAMMYA LLLVIPLFTA ILAIVVFRVA
FYGIKHNKFG FKVTAPVIAL PRLFRKDGDN KAASEKVLPG GAIIGWPEDI NKQRTVLIAT
LEYEIIDWQI KVKIGGLGVM SSLMGKAMTD VDLIWVIPKV QDVEYPAGER TEPLEVVIFG
ETYLIDVELH VYGTITYVIL DSPVFRTQTK ADPYPARMDD VFSAVFYSTW NQAIAGIIRR
FPGIDIYHIN DYHGALAPVY LLPKVIPVCL SLHNAEFQGL WPLRTKEEMK EVCSAFNISK
EHCRRYVQFG NTFNLLHAAA SFISAHQKSV GVAGVSDKYG KRSWARYPAL WTLKHVDSLP
NPDPTDIAAL DEVPVDMSGV QIDEAAEAAR PELKRQAQEW AGIKQDPDAD LFVFVGRWSK
QKGVDLIADV MPSLLEKRPS IQLVCVGPVI DLYGKFAAEK LARLVEMYPD RVFSRPEFTS
LPPFIFSGAD FALIPSRDEP FGLVAVEFGR KGALGVGSRL GGLGLMPGWW FPVESTSTAH
MISQLTKTIK LALKSTQEER AIMRARSAVQ RFPVMEWRQK IEDFHRRAIT VSRAEAGTFS
WRPEDCADPH HPRGDENEAD NSFGLDSRSD VDYSWPTTPT YAAPPSPWPT DDETYAQSPS
PYQQQFSGSY GNQYLEVPQM TPSRRGSFNS EYSDEAQPYA APYYNVVQDG PYNQFLTRAE
RQVSVDPHDL HLPPPPKIPR PDERSASTDS IVSIIDEKTD SPLNQAMTTF TDADGEVAQA
FAARLQYLDA NNSKGDLSIE KFLTKSEEAF FDRARRDKLV AAVGVHSRRN SFWSTFDEGD
PDYRPGSSTG HSMMSATLNV VFDSLEYQDN PPSTRPLTAM QMAMQRRLIG WPLYAIILAL
GQMLGATSFQ ITLLSGQNWQ GDFELYVLGG VFLVSSIVWY SLFRLKPCFY VLSAPWIFFA
IAFVLIGLPA IMPSMPQAKL VTALATWCYA VASAAAFLFF GLNFGEEAGV ATEVYTLRAT
AVQGSQQLWV AALWYWGDQL NGRLPGKTAP WWIVIILWPL SIICMGFAFC LYRGLPDFYR
QVPPKVPNFT KTLFRRKLVL WFLASEVLRD YWLSGPYGRN WSFLWGSHLP KTQILLLVLL
FFVVVWGAML LVLTHFSKTH TWLLPVFAVG LGAPRWCQML WGTSSLALYI PWAGSAGPYL
GTSLWLWLGV LDAIQGVGLG MILLQTLSRL HVCATLAYAQ VIGCICVMVA RATAPNRIGP
GSVFPDAAKW DFENGLEGSP MASAPFWLAL ACQIVIVFGY FWFYRKEQLA LVLTKVVARP
//
