ID M3B2Y2_PSEFD Unreviewed; 2397 AA.
AC M3B2Y2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=MYCFIDRAFT_44346 {ECO:0000313|EMBL:EME83737.1};
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855 {ECO:0000313|EMBL:EME83737.1, ECO:0000313|Proteomes:UP000016932};
RN [1] {ECO:0000313|EMBL:EME83737.1, ECO:0000313|Proteomes:UP000016932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86 {ECO:0000313|EMBL:EME83737.1,
RC ECO:0000313|Proteomes:UP000016932};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB446557; EME83737.1; -; Genomic_DNA.
DR RefSeq; XP_007924255.1; XM_007926064.1.
DR STRING; 383855.M3B2Y2; -.
DR GeneID; 19339586; -.
DR KEGG; pfj:MYCFIDRAFT_44346; -.
DR eggNOG; ENOG502QQX3; Eukaryota.
DR HOGENOM; CLU_000488_0_0_1; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000016932; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 2.
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 Hydrolase {ECO:0000313|EMBL:EME83737.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016932};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EME83737.1};
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..2397
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004031297"
FT TRANSMEM 1091..1117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1962..1979
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1999..2017
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2024..2046
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2058..2078
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2090..2110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2138..2160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2180..2197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2217..2238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2245..2265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2296..2317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2324..2346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2366..2389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..542
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1782..1805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2397 AA; 269582 MW; 53424F5F1A43B6A9 CRC64;
MGVWGCVVLS VLCGSSATAY KFDQAYTEVN LNQNQTAIDP LDFWGEWTGH NFTASPDNWR
FPFYTLFLDR FVNGDPYNDN YNNSAFERVT DSNQMRHGGD LQGLVDTLDY IQGMGVKGLY
IAGSPFMNAP WQYDSYSPLD LTLLDPHFGS LDMWRVAVDE IHARGMYVVL DNTFATLGDL
IGFEGYLNTT TPFTLQEHRV LWKSNRHYWD FDIGNEYTEN CTYPRFWNET GFPIDQEIKD
QMKGCYMSEF DQYGDTEAFG VYPDWRRQLS KFASVQDRLR EWQPSVRAKL EHFYCMAIAQ
LDIDGFRYDK AVQATVDAMA DMSAATRTCA RRYGKENFFL PGEVTGGNSF GSIYIGRGRQ
PDQVPDNITQ AVQLTRDSPD DYFVRGKDQV ALDGAAFHYT TYRSLTRFLG MDGNLEAGYD
GPRNWIDQWN TFLLTNDMIN ANTGVFDPRH MYGVTNQDVF RWPAIERGVE RQLLGHFITI
LLMPGIPKLL WGEEQTFHVL DSTNDNYIFG RQPMSTQTAW QTHGCYALDS SQYYQMPWDR
ARHGCNDDSV SADHRDPSAP VRNILRHFFH LREAFPVLND GFFLQQLSNQ TWEVFYAGSS
GVPTETGLWS VLRNSLPAIQ NLTSPRHGNG TRNHPQPATP VWLLYSNLNA SQTYQFDCRD
NATDLNSTSL ISPFPGGTTV KNLIYPYDEH TLMNGTQYLG MGGSTEPNGC LNKLAMKAYD
FRAYVPKSQW VGPKPVITKF LPGHDARFLS NNTDTSGIED IRLALDFSSD MECDSITDSI
SFSSKTETGI YPYIDRDSVR CGQVNESAET SWVAEIPSMF SWSATIRNVS NGIHRMTVDR
PHAVHMPQQR HNVTTESRDH FLFRVGQENN PMVFTRSANY STTLLAQSSH GQITLNHSAA
GADLYRYSTD FAGCFSEWTP YQGGVETVSA HPCANANSKS WKGEHVRVEY FSRLGGSSSH
VQQGDLHSKP RRFPHMYLNG PYNAYGYDAG LDNRMKLTDD YTWTFNWNRE WSNDGTIGQI
NVWGMGPDGT PDQRMVLGDI DGDSVLDQLP PSSLAKLVLN VTAPPSKPYL AWRLVVNDGN
LRFRLDPTGS MWWQLALYVI LWVAPLTTAA LSTYIFVGSF YKIKFNKIGV SEKLGLMGLI
PAPLRKYFPK ESADEHKSLI TKLKDSSSIF TRGSQIWSRK GEEFMNLPDT RRTVLIATME
YDIEDWNIKI KIGGLGVMAQ LMGKNLEHQD LIWVVPCVGG IEYPQDELAM PMTVAVMGKT
YDVNVQYHKL RNITYVLLDA PIFRQQTKAE PYPARMDDLD SAIYYSAWNQ CVAQALVRFP
IELYHINDYH GTVAPLYILP RTIPVCLSLH NAEFQGLWPM RTRKERDEVC SVFNLPPNVV
SEYVQYGEIF NLLHAGASYL RIHQEGFGAV GVSKKYGARA YTRYPIFWGL KEVQALQNPD
PSDTAVWDKK LPDQKDIHID EDFEEKRLND RVQAQEWAGL EPDPKAELFV FVGRWSMQKG
IDLIADAFPA ILEAHPNAQL ITVGPVIDLY GKFAALKFDR LMELYPKRVC SKPVFTALPP
FIFSGAEFAL IPSRDEPFGL VAVEFGRKGA LGVGARVGGL GQMPGWWYTV ESTTTAHLLH
QFKDAIRGAL SSPVKTRAMM RARSAKQRFP VQQWVEELEV LQSTSIRTHD KVAAEKNSWS
SSTITLVHPH PSIHPTLGSG ARHTPRGSMY GPSSHVSWDG SQSEQILDDD EIIVGDREPL
PPMATDIVRE YRESSHPFPS LRQMINDDNR SECSVHTPRC VSPIQPEDCS EPSSPGLSKP
ARTRSSMALP QNNRASTVNF STARTSIIPR TVSGLSMQNI VGEKTDFNLQ KVDPFFTDTN
GHFYRAFGRK LGTLDASNSE SSNCIEEFLV KSEKEWFTEF RNAKLGMLKR DGATTRPESI
APSEPATADN ASAKSEIHVA DFYLGDEYKP PTGLRKWMQV RVGAWPLYAY FMALGQIIAA
NSYQITLLTG EVGQSATKLY VVASIYLVAS SIWWLCFRRC ASHVSLSLPF LFYGLAFFFV
GIAHFAPTMD GRGWVQNLGT AFYTVASASG ALFFALNFGD EGGAPVKSWV FRACVIQGSQ
QLYVVALWYW GSFLSRQRAL GFQASQDSVV GTWKATAITL PIAGFLGAIC LIMWLGLPSY
YRQAPGKMPS FYKSIARRKV VLWFFVTAVV QNFFLSAPYG RNWSFLFSSI HTPAWHILLL
VLLFFIFIWA AFCALFAHLS RSHSWILPLF AIGLGAPRWA QIWWATSNIG LWLPWAPGSV
DTGAIYISSA LLSRSLWLWL GVLDSIHGVG IGMIMLGTLT RNHVAFALTA AQVLGSMATI
LGRAVAPNRL GPGPISPDIG GGLAALWSAW FWIALIANLA LCVGFYKFYR KEQLQKP
//
