ID A0A074XHG5_AURPU Unreviewed; 2371 AA.
AC A0A074XHG5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=M438DRAFT_354948 {ECO:0000313|EMBL:KEQ84940.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ84940.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ84940.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ84940.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584981; KEQ84940.1; -; Genomic_DNA.
DR STRING; 1043002.A0A074XHG5; -.
DR HOGENOM; CLU_000488_0_0_1; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000030706; 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; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..2371
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001702341"
FT TRANSMEM 1984..2002
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2009..2031
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2043..2063
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2075..2096
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2116..2137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2158..2176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2196..2218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2227..2246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2270..2290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2297..2316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2345..2363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..520
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1647..1693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2371 AA; 264130 MW; 9017DFD32AACBDCE CRC64;
MASVIFKTIS LLNLCLTLHN SQTQALDWSA DQVEWNLNQN ENATGPLEYW GEWENHPKTP
SPSNWRMPFY MLTLDRFVDG KPSNNDANGT VFENDWTTNQ FRFGGDAKGL MDNLDWIQDL
GIKAIYFSGS PFINMPWASD GFGPLDFTLL DAHHGTIDEW RQLIQELHTR GMYAIMENTI
GTMGDLLAFE GWENETTPFN AHEYDALWKS SRRYHDFEIS NDVLQDCEYP VFYGDDGFPV
NASIMATFDN QCRKSDFDQY GDMKGVGYVP PYQSQLSKFA SVQDRLRLWK HDVLEKVKHF
SCMQIAMLDI DGFRVDKALQ TPADALAEWA TYQRECARQY GKDNFLVTGE VVGELKYSSV
FFGRGKSPNT YFDNQTEAQL ATNATEGYIR ESGNNALDGS NFHYPTYGAL TRFLGLDGDI
GFEGVDFAQH WNAYLLTDDF VNVNTGLFDP RHMFGTTNQD VFRWPALVNG TQRQVLGFFI
TFLEMPGIPE LIWGDEVEFK VLENLAADYM FGRQPMASTR AWQMHGCYKV GAAGNGYYDM
PFGDALLACQ DDSVSLDQRN PAHSLRNLIK RMFQLRTHYP VLNDGFTLQT LFFETHDVFL
PHSGQLPTPL GIWSVYRGRT PGVQDFTGEG MGNQGIWLLY SNQNETVHYS YDCSNSSGSL
VAPFPEGTTI KNLFYPYQEY TLNSSTTKLG IEGSDEINGC LPGIELEAWG FRAFVPIDKF
VAATPVISGA IPRHDARIET TADFNDVIAV PVTLSFTQAM DCSSILKSIS FESTTQTGIV
PHFEASSVVC RNITVDNSQR FVGEALSTFQ WSANLVNLSH GVHTYTVANA SSADGISFTN
TKDKFMLRVG LKDNPVVFPS SANYTTGLVH RDATTGELRV TPKAAGSTQW RFSTNYGSSW
SDWTSYTGET TTIEEQAWSG TSAQQWSGVH IVTQYYSPLI GSTDHVQHSD LDAEVPRRWP
KVHVQGPWNQ YGYDAGLNDQ MKQDSEGIWN FDLSSEWPTS VILNVWGMNP DGAPDKSAAY
GDVDGDNVLD WVPPDSLSFN QLNITPPSWP HTAYKIAVND GSMRYTITPT GSANRQLALY
ILLATLPLIT ACLAVAIYHG SFYRLKYNSI GLTKRSYPFN QFQKKRSVSD ILPLSFTKIS
EKQDATDAPE ASDGAVITTE TSRTILIATM EYAIADEWNI SIKIGGLGVM AGLMAKHLTH
HNLIWVVPCV GDVVYPIDRV MEPIKITVMG KPYLIDCQIH VVGRITYVLL DAPLFRQQTK
KEPYPARMDD LDSAIYYSAW NACIAEVMRR HPEIDIYHIN DYHGAVAPLH LLPRVIPVCL
SLHNAEFQGL WSINTPKKMQ EMSDVFNLDK SIIRRYVQWG DNFNLLHAGA SYLRIHQKGF
GAVGVSKKYG ARSFARYPIF WGLPKIGILP NPDPADIEHF DKCLPNPDVA IDREYEASRG
ATRKQAQQWA NLNIDESAEL FVFVGRWSMQ KGIDLIADVF PKVLEENPKA QLICVGPVID
LYGKFAALKL DYLMKKYPGR VYSKPMFVYV PPFVHAGAEF ALIPSRDEPF GLVSVEFGRK
GALGVGAKVG GLGQMPGWWF QIESSMTRHM LSQFKKCIQA ALSSDQETRA LMRARSKEQR
FPVAQWVEDL EILQTKAIKI NTKVQDGSVS ALSTPNSTPN SSPPRSRAQS RVASPAASRS
SSPTPETPAP QFRRRLSSLL YPVHPTAEQY MPFRRRLSSL FPMSRRSPFQ HSEAGADISE
LEESRDEVGS LPPSSPTFRP GTAGSMSAAH ALFTPGFGFA EEQNLPGELT RPTLAHYRRS
STLSVDEVVG EKTDYSLQKV DQSFTDSQLD YYRIYETMLG SLTAKNSEGK LCIETFLHSA
EKNWYRRFGE AKLGRTVVSP PEVGSKKFGA KGVSVTVREA SSISESERTA SVGAMSHTSA
EQFFTTANYK APTGISKLMM SKIPYLAPDW PLYAYLMAFG QIIAVNSHQI TIITGAQGEN
ANKLYTIASI YLAGSLFWWL MIRRLASKWA LSLPFVLYGL AFVFVGLAPF GTTLDSRGWI
QNVGAGLYSF ASASGSLYFA LNFASEGGVP IQTMIFRATA VQGVQQLWVA ALWAWGSAMS
ANHTSQFTNT IMNSKVLLAI MAPIALLFVS VGVILLFGLP EYYHNSPGKA PSFYTSVWKR
KIVLWFFVAI IAQNYWLSAP TGRNWQYLFS STQAPVWSIV LLLLLFFIVI WCVALYTLSR
FSGHHSWFLP IFGAGLGAPR WCQMLWSTSG MGLYLPWGST LGSAIAGRSL WLWLGTLDAL
SGVGIGTMLL QTLTRHHVAV TLTAAQVLGS IATIAARASS PDATGPGAVF PNLAVSLAGL
GAWEFWVALL FQLVLPIGFL MFFRNEQLFK P
//
