ID A0A319CWQ2_9EURO Unreviewed; 2421 AA.
AC A0A319CWQ2;
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=BO71DRAFT_488238 {ECO:0000313|EMBL:PYH89079.1};
OS Aspergillus ellipticus CBS 707.79.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH89079.1, ECO:0000313|Proteomes:UP000247810};
RN [1] {ECO:0000313|EMBL:PYH89079.1, ECO:0000313|Proteomes:UP000247810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH89079.1,
RC ECO:0000313|Proteomes:UP000247810};
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 (FEB-2018) 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; KZ826049; PYH89079.1; -; Genomic_DNA.
DR STRING; 1448320.A0A319CWQ2; -.
DR Proteomes; UP000247810; 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 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:UP000247810};
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..2421
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016272080"
FT TRANSMEM 1074..1096
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..2075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2087..2108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2120..2141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2161..2187
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..2266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2320..2340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2347..2370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2393..2413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..520
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1649..1673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1799..1837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1939..1964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..1668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1810..1831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2421 AA; 270198 MW; 0F81B622871AE11D CRC64;
MKWASSGSLL ALLAASATAW PYNESLVDYN FNTNQTATNP ADYWGEWPNH TDQYHPSPDN
WRFPVYTIFL DRFVNGDPSN DNINGTLFEH DISQTQMRHG GDVVGLVDSL DYLQGMGVKA
LYIAGTALMN QPWGYDGYSA LDTTLLDQHY GTLQVWRDAI TEIHKRGMYV IMDNTIATMG
DLIGFDGYLN TTAPFTVKEH QVVWKSDRQY VDFRFGNTYN DTCDYPRFWF ENGYPVQQSV
DDSLVGCYDS DFDQYGDVEA FGVFPDWERE LAKFASVQDR LREWHPSVRE RLIRHSCMII
YQLDIDGFRY DKATQSTVDA LGDMSSAYRE CARAVGKENF YIAGEITGGN TFGAIYLGRG
RQPNQYPSTA EEAMNMTNTS DSQYFLREVG LNAIDGAAFH YSIYRALTRF LGMDGNLAAG
YDLPVDWVDA WNTMLTSNDL INPNTGKFDP RHMYGATNQD VFRWPTVEKG VARQLLGQYI
TTLLLPGVPL LLWGEEQAFY ILDATAANYI YGRQSMSPAT AWRDHGCFSL ESSQYYKWPI
ESGREGCHDE TAAYDHRDPS HPVRNIIKHM YQMRSQFPVL NDGYTLQRLS NMTEDVYYPG
SDGVATETGM WSILRNVDAN VQDLGSDDAN QPIWLVYQNT NRTIAYTFDC TDNDTALIAP
FDTGTTVKNL FYPYDEHKLV SSTQKLGING STEYNGCLAN MTMDAYEFRA YVPLAKFTKA
GPMVTGFTPG HDYPLRSTVA PNADETVSIE LYFSEAMDCD SVTSAMSFNS STEIGKTPTL
DTASVSCKTI TEGNTSYTGQ LPSNWKWTGN LTGVYNGVHR ITVSNASSSG NETTNAVDHF
LFRIGQVDNP MIFSSANYST SLLHEDTNGT LFVQHHAAGA DKYRYSTNWG TTFSDWLTYT
GGNDTIDKLA WSGTTKQSWS GEHVRVEYWN RLTGSSDYHQ EGDTGWSSNW PRRFPHVFFN
GPFNEYGYDG GLNNIVKQDT VDGLWKFHFT NEWPAVAQLN IWGMDPNGDP DQSWVLGDAD
NDSVLDRMPP SSLSATLINI TEPPPHPYIA WRVFIDDGTL RFQLFPVGHQ NTQIAMFVLF
WIIPVLTGSA CVYIFMKSFY KVKFNQVGVS EKTNMIPLAL RRKFKRARGG QDDRLNPLMR
LANKSGFLQE GTAIGGAAAS GKRRMVLIAT MEYDIEDWQI KIKIGGLGVM AQLMGKTLGH
QDLIWVVPCV GGVDYPVDTP AEPMNVTILG NSYEVQVQYH VLNNITYVLL DAPVFRQQSK
SEPYPARMDD LNSAIYYSAW NQCVAEACKR FPIDLYHIND YHGSLAPLYL LPGTIPACLS
LHNAEFQGLW PMRTQKEKEE VCSVFNLDIE TVRHYVQFGE VFNLLHSGAS YLRVHQQGFG
AVGVSKKYGK RSYARYPIFW GLRKVGNLPN PDPSDVGEWS REQAQAMSDN VTVDADFEGG
RAELKRQAQE WAGLEQNPDA DLLVFVGRWS MQKGVDLIAD VMPAVLEARP NVQLVCVGPV
IDLYGKFAAL KLDHMMKVYP GRVFSRPEFT ALPPYIFSGA EFALIPSRDE PFGLVAVEFG
RKGALGIGAR VGGLGQMPGW WYNVESTATA HLMHQFKLAI DAALSSKTNT RAMMRARSAK
QRFPVAQWVE DLEILQTTAI QVHNKELVKT HGRPHTPSGT TAPSGILSQP LSPLALPGIQ
TPLAHSRDSS YSNLNRLSEY VSDPKTNYSR DPSPGGTEKP KSGLHRQLSL GVRSGPGHQA
RQARRGRQRD SIPEQDDAGA MTDVEDDRED DMVAALYAAD DDEYTLTPAQ VEEGRRLQAQ
GGLMPSSPGD RRLSQDSRFG QMPSSPGAIP SASQGLLPPP RVLDPANNRL SSASVLSLDS
VVGTKTDFKL QKVDPFFTDG TGEYYRAFDK RLGDLSGSNS ESQLCIEEYL IKSEKEWFDK
FRDARLGRLK SPASSIYRDK HGAASPAPSL YDDGGSRLST GSASPTLEDD EFLLGKDYVP
PTGLRRWMQI RIGDWPIYSL FLALGQIIAA NSYQVTLLTG EVGETAEKLY GIATTYLITS
ILWWLVFRYF KSVICLSAPW FFYGLAFLLI GSAHWETTSF NQGWIQNIGS GCYAAASSSG
SMFFALNFGD EGGAPVETWI FRACLIQGFQ SAYIIALWYW GSTISKASSE GLVTSTSGIA
STWKMTAICY PIAIALWAVG LLIYFGLPNY YRQTPGKVAS FYKSVFRRKI VIWNFVAVIL
QNFFLSAPYG RNWGFLWTST HTHPWQIVIL CIVFFGFVWA GFLFIVSHYF NSHSWFLPVF
ACGLGAPRWA QIWWGISGIG YYLPWVSGGY VGGALASRSV WLWLGVLDSI QGLGFGIILL
QTLTRMHMLF TLICSQVLGS IATICARAFA PNSVGPGPVS PDPTFGAVAV ADAWFWVALF
CQLLVCAGFL LFFRKEQLSK P
//
