ID A0A319C1Q0_9EURO Unreviewed; 2420 AA.
AC A0A319C1Q0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=BO82DRAFT_422169 {ECO:0000313|EMBL:PYH78127.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH78127.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH78127.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH78127.1,
RC ECO:0000313|Proteomes:UP000248340};
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}.
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DR EMBL; KZ821732; PYH78127.1; -; Genomic_DNA.
DR STRING; 1448315.A0A319C1Q0; -.
DR VEuPathDB; FungiDB:BO82DRAFT_422169; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000248340; 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 CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1.
DR CDD; cd06174; MFS; 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:SF1; ALPHA-1,3-GLUCAN SYNTHASE; 1.
DR PANTHER; PTHR47182; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE AGS1-RELATED; 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:UP000248340};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2420
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016359598"
FT TRANSMEM 1071..1093
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1995..2017
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2029..2046
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2053..2072
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2084..2107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2119..2140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2165..2190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2210..2227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2247..2269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2289..2307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2319..2339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2346..2369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2389..2411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..522
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1662..1834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1933..1969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1749..1763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1933..1957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2420 AA; 271100 MW; 8D074BF357FEFAE8 CRC64;
MKWGVSGCVA ALLAATVSGW PYEESLVDYN LNVNNDTTNP AEYTAPSWPG HKYTPSPKNW
RFPFYTLFVD RWVNGDPTND NINGTLFEHD LDSTQMRHGG DAVGLVDTLD YLQGLGIKGI
YLAGTILMNQ PWGSDGYSAL DTTLLDQHYG TIQTWRNAID EIHKRGMYVL FDNTIATLGD
LIGFENYLNV TTPFSVKEHQ TIWKSERQYV DFRPGNNYND TCDYPRFWNE TGYPVDQSVR
DELVGCYNSD FDQYGDREAF GVYPDWQREL AKFASVQDRL REWHPGVRER IKVHSCNIIK
ALDIDGFRYD KATQSTVDAL GDISSHYREC ARSVGKNNFF LPGEITGGNN FGSIYLGRGR
QPNQYPKSAM DAMAMTNKSS QQYFLRENDL QALDGAAFHY SVYRTLTRFL GMSGNLAAGY
DTPLDWVDSW NIMVQSNDLI NAETGKFDPR HMYGTTNQDV FRWPAIQYGV ERNLLGLFIT
TLQMPGIPLL LWGEEQAFYI LDATADNYVY GRQAMSPATA WRTHGCWALD ATQYYDWPIE
QGRQGCHDPK VAYDHRDPSH PVHNIIKHMY QLRQEFPILN DGYSLQTLSK QTRDIVYPGS
NGTATETGMW SILRDRVSSL QNLGDEGGNM PVWLVYQNDN KTVEYKFDCG SNASALISPF
TTKTTVKNLF YPFDEHTLKS GPKALHLNGS KELNGCLDSI TLKPFEFRAY VPKAQFVDPR
PMITKFNPGH DAPLLSTVAT GESEDINVSI EFSTAMDCDA VTKAISFTSQ TESGKTPSID
KGSVDCQTMT ANDTQYVAQL PSAWSWSAKL TGVYNGVHRL TVKNATGSGS KSTQSTDHFL
FRVGQSNNPI VFTSANYTTD LMHGHENGTL YVQHRAAGAN KWRYSTNWGS SFSAWMNYTG
GNATIDELPW SGTDKQKWQG KHVRVEYWSQ LTGSSDYVQE GDYDWNGPAR RFPHLFFNGP
YNQYGYDAGL NNVAKQDSDG FWNFRVIAEY PAQGQFNVWG MNPDGKPDES FVFGDVDGDG
VLDRMPPSSL SKLSVNITDI PPSPYLVWNV KVDDGTMKIN LVPTGSRIAQ MIIYIILWVV
PILTAIAVVY AFMKSFYQVK FNQVGVMEKK SFLGMILGNK GSRDGQSSNP LIRFANKSGF
LQSTSAFGAA ASRTRTTLIA TMEYDIEDWG IKIKIGGLGV MAQLMGKHLG QQNLIWVVPC
VGGVEYPVDQ PADPMFVTVL GNSYEVKVQY HVIKNITYVL LDAPVFRQQS KAEPYPARMD
DLDSAIYYSA WNQCIAEAIK RFRIDLYHIN DYHGSIAPLY LLPQTVPVCL SLHNAEFQGL
WPMRTQKERD EVCSVFNLDI YTARRYVQFG EVFNMLHAGA SYLRVHQQGF GAVGVSRKYG
KRSYARYPIF WGLKKVGNLP NPDPSDTGEW NKQLPKDSEI EVDPLYEASR GELKRQAQEW
AGLEQNPNAD LLVFVGRWSM QKGVDLIADV MPAVLEARPN VQLICVGPVI DLYGKFAALK
LDQMMKVYPG RVFSKPEFTA LPPYIFSGAE FALIPSRDEP FGLVAVEFGR KGALGIGARV
GGLGQMPGWW YNIESTTTSH LLHQFKLAIA SALNSKPQVR AKMRARSAKQ RFPVAQWVED
LEILQSTAMR IHSKGLSKSN SQPLTPSGYN TPSGLMTPTI ASSGAITPSG VQTPPLTHSR
EGSYSNINRL SAYGPQQRNT IVYSRDPSPG ANEKPKSGLS RTLSLGVRSG PGHLVRRGRR
RLRRSMGHED PANNSNTEES SDDDFIPSYY GEEEYTLTPE QAEEGRRNDA TPQLDMPRQT
PPRDFFSRRQ SSQSSLTPRP ILTTTSPGSP EPEEALVSPV RQYANEPGNR LSSASVLSVD
TIIGEKKDYK LQKVDPFFTD STGEYYKAFE KRLENLNGSN SESQLCIEEY LMKSEKKWFD
RFRDARLGRN QSPASSVFNA KMDNNSPMSS VRADEMGSQE SRSPERREKD EFLLGNDYVP
PSGLRKWMQI RIGDWPLYSF FLGLGQIIAA NSYQITLLTG EVGETAEKLY GIATVYLVAS
IVWWFFFRSF KSVFVLSLPW LLYGLSFVII GVAHFETDAF ARGWIQNVGA GVYAAASASG
SLFFALNFGD ENGAPVKEWV FRACIIQGCQ QAYIIGLWYW GTAISQAVES GATNVQGDIT
NTWKMTAICL PIAAFLWAIG LLLFFGLPSY YHQTPGKVPS FYQSVFRRKI ILWNFVVVIV
SNFFLSAPYG RNWSFLWSSA HAKPWEVGVL CVVFFGFIWA AWLFLFGYLS KTHSWILPVF
ACGLGAPRWA QIWWGVSGIG LFLPWAGSYT SGALVSRAVW LWLGVLDSIQ GLGFGMILLQ
TMTRMHICFT LLASQVLGSI ATICARAFGP NKIGPGPISP DITAGVSSIA NAWFWIALFF
QLLICAGYLM FFRKEQLTKP
//
