ID A0A0C4EJL1_PUCT1 Unreviewed; 1839 AA.
AC A0A0C4EJL1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
OS Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=630390 {ECO:0000313|EnsemblFungi:PTTG_00929P0, ECO:0000313|Proteomes:UP000005240};
RN [1] {ECO:0000313|Proteomes:UP000005240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|Proteomes:UP000005240};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Fellers J., Bakkeren G., Szabo L., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblFungi:PTTG_00929P0}
RP IDENTIFICATION.
RC STRAIN=isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|EnsemblFungi:PTTG_00929P0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
RN [3] {ECO:0000313|Proteomes:UP000005240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|Proteomes:UP000005240};
RA Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA Young S., Zeng Q., Fellers J.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblFungi:PTTG_00929P0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|EnsemblFungi:PTTG_00929P0};
RX PubMed=27913634; DOI=10.1534/g3.116.032797;
RA Cuomo C.A., Bakkeren G., Khalil H.B., Panwar V., Joly D., Linning R.,
RA Sakthikumar S., Song X., Adiconis X., Fan L., Goldberg J.M., Levin J.Z.,
RA Young S., Zeng Q., Anikster Y., Bruce M., Wang M., Yin C., McCallum B.,
RA Szabo L.J., Hulbert S., Chen X., Fellers J.P.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL G3 (Bethesda) 7:361-376(2017).
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; ADAS01000656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADAS01000657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 630390.A0A0C4EJL1; -.
DR EnsemblFungi; PTTG_00929T0; PTTG_00929P0; PTTG_00929.
DR OMA; ESTNTHG; -.
DR Proteomes; UP000005240; 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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005240};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1012..1035
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1784..1805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..474
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1497..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1585..1619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1839 AA; 205677 MW; F5E7C39237F14AB6 CRC64;
MEVDIPPAQL TGGSCQSIPF MDGNPSNNDF YKSRSEWDFL SNQLRHGGDI EGFAQDRVLD
YIYGMGYRTI YIAGTPWLNM PWQSDGYSAL DFTLLDPHFG TLSEWRAAID KIHSKGMYVM
LDTTTTTLSD FLEFKGNSGK AAPFNLHGYE VEYKTTVQKP WNINQYAEFQ FTNSRDQSCR
LPKFYNPNGT DVLPPADWDG CYAGDFNQFG DSSPAGKAPG WQDQLTKYSG VQDRLRDWDS
GVAAKLEKLA CMTVKALDMD ALRVDKATQQ TLEFMGKWGG ALRTCAKDLG KNNFFITGEI
SDGNTFGSLY IGRGRQPAHY ANLQFDTAAL VTANQTENFM RPVGENALDS AAFHYSIYRS
LTRFLGMDGE LDSPYDIPVN WVEAWREIFV TNDLLNQETQ QLDPRHLYGT TNQDNFRWAS
LINGTERFLL GQLVTNLIMP GIPFAFYGEE QDLHIFDSQA NDYLYGRQPM SSSKAWQAHG
CYKLGSKKYP TMPLGKALNG CKDDWNSLDH YDPTSNTRNM LGHFAYLRSQ YSSLQDGFNL
TQLGNWTTFG ELPASSHTPT EWGLWSVSRS PLKSQKLSGP NPELPVWILY SNVNQTTTFS
YDCASKLAIT SPYPAPSTVR NLFYPYETYD LDPSSTSSTW DEAPPFLGCL KSITMEPLSY
KALVPASNWT PPQPRLVGFT PGHDARILSQ ADNDNETIPI SFSFSDELLC EGVSSSLSLS
YTIDPNSKAS PRIDLEHANC SKIESSSNST QNALPAVWQW SASIVGAADG IYELVLNNAT
GQNGIHTNSI DHLLLRKGRK QNPITFSDVS YPESLLESKD GKYTLRSDAP GADLMRYSID
FGKTYSNWTR YSSELTLPDN AFSISKFWEG DHVRVQYWSR LAGSAAAAID ADINFAGGYK
RKFPQLILRG AYNKWGFDEG IPGLLSPRSE NMTIDVITSW PHEFQLAVFE AREKVFYGDV
DNDGVLDLLP PNSQARNFLS LPPPSKPYLG WRIMINPKDL TWGAQPVGHQ KIVIMLLILF
LFIPPTTALL ACWLYQRIFY KVKHNQHLPK SMRNSRIPST LKHVITPHFG SNAEKSQASF
ANTWPDNAGS RRKVLIATLE YEIIDWGIKV KIGGLGVMTS LMGKVMEDLD LLWVIPKVSG
LEYPEAERAE PIAVVVFGET YLVELQIHKF KNITYFLLDS PIFRANSKIN PYPARMDDLD
SAIFYSYWNQ SIAEICRRTP DLTIYHINDY HGALAPLYLL PKIIPVSLSL HNAEFQGQWP
LGTPEEENEV CRSFNISSKV CSKYARYGSV FNLLHSAASY ISHHQNSVGV AGVSEKYGKR
SWARYPVLWT LKSIEPLPNP DPTDVESLDV TPPDMRRIQI DQEAEAERPG NKLKLQEWAG
LHEDPKAQVF VSDEPFGLVA VEFGRKGALG VGSRLGGLGL MPGWWFPVES DSTAHLHSQF
AKTLRAALEC PEEERAVLRA RSVHQRFPVL EWRIKMEDIH ARSVRASRKY AGRLTMNTNP
TEVIKSDESS SVSHDQGKPV QVHPPSSESN KTGVICTPST KNPTNTFGSQ LNHTRPSLDV
SRMLSSSHQL AVQLSEAVKR LIITKRGSST HPSRPSEQRT ESAPLDGAVT PSERPQNNDQ
EILTSTIITL DKNNGNTGEH NPADFQRTYC GQDDKNSPLN QGLKDFTDED GKASQEFVRR
LQKLDASNSR SELCIARYIV AAHKEHFNQV RKGTLALART RYASSPTLSV TSIIPRTMLG
GGISSPTNGL HDISDQVKNE KSDTLDVTAA LSMNLWQIRL QRRVFGWPIY TILLAIGQIL
GATSFQLSLL SGTSSNGSFD FYGSCCRTSP GEFLVRFQN
//
