ID B8N2R2_ASPFN Unreviewed; 2345 AA.
AC B8N2R2;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=AFLA_023460 {ECO:0000313|EMBL:EED55075.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED55075.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED55075.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963473; EED55075.1; -; Genomic_DNA.
DR RefSeq; XP_002373857.1; XM_002373816.1.
DR STRING; 332952.B8N2R2; -.
DR EnsemblFungi; EED55075; EED55075; AFLA_023460.
DR VEuPathDB; FungiDB:AFLA_000184; -.
DR eggNOG; ENOG502QSGC; Eukaryota.
DR HOGENOM; CLU_000488_0_0_1; -.
DR OMA; AWRDHGC; -.
DR Proteomes; UP000001875; 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; 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 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}; 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..2345
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002877821"
FT TRANSMEM 1075..1097
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1919..1941
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1953..1970
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1977..1995
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2015..2032
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2044..2064
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2094..2115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2135..2154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2166..2190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2199..2220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2244..2264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2271..2293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2313..2336
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 1648..1773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1797..1856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1869..1896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..1676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1742..1768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1831..1845
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2345 AA; 263060 MW; FDCB7ABE425D5E0E CRC64;
MKWAFSSAVL ALFATTVKAW PYEESLSAYN LNENKSATNP AQYWGEWPDH KGKYFPSPDN
WRFPVYTLFM DRFVNGDPTN DNINGTLFEH DISSTQMRHG GDVAGLVDTL DYLQGMGIKA
IYLAGTILMN QPWGSDGYSA LDTTLLDQHF GDIATWRNAI DEIHKRGMYV IFDNTIATMG
DLIGFEGHLN DTTPFSVKEH KALWKSNRRY VDFDIGNDYN QTCDYPRFWY EDGYPVQQSM
TEGLVGCYDS DFDQYGDIEA FGVFPDWQRQ LAKFASVQDR LREWHPSVRE RLIRHSCMII
YQLDIDGFRY DKATQSTVDA LGDMSMAYRE CARAVGKENF FISGEITGGN TFGSIYLGRG
RQPNQYPETA EKAMKMTNES ESQYFLREAG HEAIDGAAFH YSTYRALTRF LGMDGNLAAG
YDVPVDWVDA WNLMLQSNDF INPNTGKFDP RHMFGATNQD VFRWPTVEKG VERQLLGLYI
TTLLLPGIPL LLWGEEQAFY ILDATASNYI YGRQAMSPAT AWRDHGCFSL DSSQYYQWPI
QAGREGCHDP TAAYDHRDPA HPVRNIIKHM YQLREDFPVL NDGYSVQKLS NLTEEVFYPG
SNGTATETGL WSILRDVNAD VQDLGSDAKN QPVWLVYHNT NRTIDFKFNC KDNETALISP
FATGTKVRNL FYPYDEHTLI DGPVKLGLNG STELNGCLAN MTLDAYEFRA YVPSARFTKP
RPMITQFTPG HDVPVRSTVA PNLDESVKIE LYFSEEMDCD SVTKAISISS STESKKVPTL
DEKTVDCKGI PASNTSWTGQ LPSVFMWAAN LTGVYNGIHR VTVKNASSTN GNATTNAVDH
FLFRIGQIDN PMVFTSANYS TSLLHEESNG TLFIQHHAAG ADKWRYSTNW GTTFSEWKDY
TGGNDTITEL EWSGTKKQRW KGHHVRVEYW SKWTGSSDYV QEGDAGVHSN VPRRFPHIFF
NGPYNQYGYD GGLDNVVRQD SKDGLWKYHF TAEWPAQAQL NIWGMNPDGK PDQSWVLGDA
DNDSVLDRMP PSSLSATLIN ITEHPPKPYL AWNIYINDAT MKFQLFPVGH QNTQIAMFVL
FWIIPVITGA ACVYIFMKSF YKVKFNQIGV SEKATLIPLA LRRKFKRNRG GDEERMNPLM
RLANKSGFLQ TNTAIGGAAS GKRRMVLIAT MEYDIEDWQI KIKIGGLGVM AQLMGKTLGH
QDLIWVVPCV GGVEYPVDKP AEPMNVTILG NSYEVQVQYH VLNNITYVLL DAPVFRQQSK
SEPYPARMDD LNSAIYYSAW NQCIAEACKR FPIDLYHIND YHGSLAPLYL LPDTVPACLS
LHNAEFQGLW PMRTQKEKEE VCSVFNLDID IVRRYVQFGE VFNLLHSGAS YLRVHQQGFG
AVGVSKKYGK RSYARYPIFW GLRKVGNLPN PDPSDVGEWS KEKAIGNADE VHVDPDYEAG
RADLKRQAQE WAGLDVNPDA DLMVFVGRWS MQKGVDLIAD VMPAVLEARP NVQVICVGPV
IDLYGKFAAL KLDHMMKVYP GRVFSRPEFT ALPPYIFSGA EFALIPSRDE PFGLVAVEFG
RKGALGIGAR VGGLGQMPGW WYNVESTATS HLLYQFKLAI DAALNSKQET RAMMRARSAK
QRFPVAQWVE DLEILQTTAI QVHNKELVKH NGRPFTPTGT TTPSGLMTQP ASPLGTPGMQ
TPLAHSRESS YSNLNRLSEY VTQPKTSYSR DPSPSGTEKP KSGLQRQLSL GVRSGPGHQS
RRGRARQRDS IPEHEDTQEA HGGAITDVEE ESSDDDIVNH YADDEYTLTP AQVEEGRRLQ
AAQQQAGIRM PLSPGGRRYS QDSLHPRNVQ PPSSPGTPPA ASQSLLPPPR LLDPGSRLIY
RDKHGASPIG SFYDDNGSRM SGSDGPHSND SEDDEFLLGK DYVPPTGLKK WMQIRIGDWP
IYSLFLALGQ IIAANSYQIT LLTGEVGQTA EKLYGIATTY LITSILWWLV FRYFKSVVCL
SAPWFLYGIA FIFIGSAHFE SNSFTRGWIQ NVGSGFYAAA SSSGSFFFAL NFGDEGGAPV
ETWIFRACLI QGIQSAYVIA LWYWGSTLSQ AQSEGLLTPT NNISNSWKMS AICYPIAAAL
FGIGLLLTFG LPNYYRQTPG KVASFYKSVF RRKIVLWNFV AVILQNFFLS APYGRNWQFL
WTSHHAHHWQ IVILCVVFYG FVWAGFLFVV SRYFKSHSWF LPVFACGLGA PRWAQIWWGV
SGIGYYLPWV TGGYTGGALV SRSVWLWLGV LDSIQGLGFG IILLQTLTRM HMLFCLVCSQ
VLGSIATICA RAFAPNNVGP GPVSPDPTFG GSAVANAWFW VALFCQLLVC AGYILFFRKE
QLSKP
//
