ID A0A317V009_9EURO Unreviewed; 2391 AA.
AC A0A317V009;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-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=BO94DRAFT_628859 {ECO:0000313|EMBL:PWY67644.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY67644.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY67644.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY67644.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWY67644.1}.
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DR EMBL; MSFK01000047; PWY67644.1; -; Genomic_DNA.
DR STRING; 1450535.A0A317V009; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000246702; 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 CDD; cd11323; AmyAc_AGS; 1.
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; 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; PF13692; Glyco_trans_1_4; 1.
DR Pfam; PF08323; Glyco_transf_5; 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:UP000246702};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1069..1091
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1966..1983
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2003..2020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2032..2051
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2057..2081
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2093..2114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2134..2161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2181..2198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2218..2237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2318..2340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2363..2383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..536
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1685..1803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1910..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2391 AA; 268181 MW; 7770BE7486A37D61 CRC64;
MFRMDWQRSA VLIVGLLSVV AVGWPYTESL ADYNLNTNSS AKSPIDYWGE WPDHEYHPSP
DNWRFPMYTI FLDRIANGDP TNDNINGTTF EHVIDSNQMR HGGDLVGLID SLDYIKGMGF
KAIYFAGTYL MNLPWAYDGY SPVDTTLLDM HHGTLEDWRT TITEIHKRDM YVIVDNTLAT
LSNLIGFKGH LNDSADFLAT EYEVEWITDR QYVDFQFSNE YNETCNYPKF WNETGYPITT
GGVQDLKGCY NSDFDQYGEL EAFGNFPDWK RQLTKFASVQ DRLREWHEPV RNVITHHSCI
QIASLDVDGF RFDKAVQGTL EPLADIISTY RECAKKYGKH NFFLPGEITS GNTFGSLYLG
RGRQPNQVPD SVDVAIKLTN DSDSEYFLRD DGLQALDSAA FHYTIYRSMT RFLGMDGNLV
AGFDLPTDFI EAWNGMLETN DFINAFTGEL DPRHMFGVSN QDNFRWPAIK NGTVKYLLGL
YIVTLELPGI PLVLWGEEQA MYVFDATASN YLFGRQPMTY QTAWWTHGCF SLNTSKFYDF
PNDKGLNGCN DITVTYDQRN PAHPLRNIMK RMFEIREQYP VANDGLYLET LSQLTENIYL
PGSETTPTVT GLWSVLRTYY PGVQQNATQS NGTLWLVYQN GNTTETYGTS CTNKTAALLA
PFDSGKKLKN LFYPYDELTL EDGPGGSGAY GCARNMTLLP WEYRAYVEAS SFVEPGPTVT
EFVPGHDARL ISSEDNGESL AIQLGFSKPM DCDVLTKAIS LNSTTTKGIT ASFDTSNVTC
ANITARTTSN NFVGEVPTVW TWSTTLKNVY HGVHQLTVNN VTSVNGTHTN AVDKFLFRLG
TETNPLISPL ANYSTTLLQK SDNGSYYIQH DAAGADKYRY STSFGSSWSN WTEYTGGNTT
IDLTSWSGTS AQKWKGTHVR VQYFSRLTGS SDYLQEGDYG WKDGVARRFP HMWWNGPYNQ
YGYDAGLDSK MRFDEDDLRW KYDFVYEWPS VGQISIWGTD EDGTPDTTGV YGDVDNSSVV
QRLPPSYLSS NVINITELPP FPHLGWTISL NDANLRYELI PVGSGWAQLV LYVLLWVVPI
LMALAGVFIF IRTFYRVQLN TDGNVAKEDK LPLLVWRRLR GQSGDDHSER AVSAMAAAAP
STEMAIAGAP EKRRTVLIAT MEYDIEDWKA KVKIGGLGVM AQLMSQHLGH QDLIWVVPCV
GDIEYPQDTP TEPYIVTILD NPYLVHVQYH VLNNITYVLL DAPVFRQQTK AEPYPPRMDD
LDSAIYYSAW NQCIAETIKR FPSIDMYHIN DFHGCLAPLY LLPSRTIPVC LSLHNAEFQG
LWPLRNQQEK KEVCSVFNLP VETATKYCQF GTVFNLLHTG ASYLRFHQRG FGAVGVSNKY
GKRSWARYPI FWSLEKIGSL PNPDPTDIAP LEESGDEKAL TRSYEERITD KLEAQKWAGL
TEDRNADLLV FVGRWSKQKG VDLIADVIPA VLSARPQVQV ICVGPIIDLY GRLAAIKLDK
IATMFPGRVF SRPEFTVLPP CVFSGADFAL IPSRDEPFGL IAVEFGRKGA LGIGSRIGGL
GQMPGWWYTV ESDATRHLLH QLRTAIKSAL DSSQETREQM RANSAKQRFP VLEWIQKLET
LQRTSIQIHH DKNKATVAGS LPESQSAWDL QQNMRYSTLA LPGTQSRASG VETPPETVIE
HAQSRLQELQ TAEGNSRASS LNRQLSLGRR AGPGQGRNRL TKRQLSTHSP GDETTDAEDD
DENAAPPVDY ISPEEAMRAV TSTLAPTPGG DSRASVSTPP LIPPPTFRNS RPGSPYPISQ
VSSPSLAPPM GHFRTVSMLS LPSVVGDHTS FVGESTPTQN QPVFELQKVD PTFTDSMGHF
TRRFEDILTK LNKKNSVTDC CIETYLMKSE RQFYYDYSDA QLKKQPKDRA IAMPGSDSGM
HDGPDGRASY ASANSDSDGT DEIDRWLMQL GYRRPMVIQR FMRRRIGNWP IYSLFLGLGQ
IIATNSSQIT LLVGQVGETA VKVYVIAAIY CVSSIAWWFI YHRSPAVFSL TLPWFLYCLA
FIIIGVSPFG LTSLGRAWAQ NVAAGVYAIA SSSGSLFFAL NFGDQGAVPV KDWMFRASMI
QGIQQIYTVA LWFWSSKVTA AEVGGVSVAA LSSWRLTAVV MPIAALCFAI GVLLALGLPN
YYRQSPSRIL SFYTSLFRRR IILWFFFMVI VQNWFLSAAV GRNWSFLWSS KHAKPWEIVI
LIVGFFIVLW VLILILFRAL SKEHSWILPV FGLSLGAPRW AQTWWGTSNI GYYLPWAGSL
VSGSIASRCL WLWLGVLDEI QQVGLGMILL QTMTRVHVCF VLLAAQSLGS IATICARGFA
PNKIGPASIS PDVGTSIDKV GNAWFWIALF FQLLASFGFL LFYRREQLNR P
//
