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Database: UniProt
Entry: A0A0C4F0G5_PUCT1
LinkDB: A0A0C4F0G5_PUCT1
Original site: A0A0C4F0G5_PUCT1 
ID   A0A0C4F0G5_PUCT1        Unreviewed;      2211 AA.
AC   A0A0C4F0G5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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_06582P0, 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_06582P0}
RP   IDENTIFICATION.
RC   STRAIN=isolate 1-1 / race 1 (BBBD)
RC   {ECO:0000313|EnsemblFungi:PTTG_06582P0};
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_06582P0}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=isolate 1-1 / race 1 (BBBD)
RC   {ECO:0000313|EnsemblFungi:PTTG_06582P0};
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; ADAS01006850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADAS01006851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 630390.A0A0C4F0G5; -.
DR   EnsemblFungi; PTTG_06582T0; PTTG_06582P0; PTTG_06582.
DR   OMA; WRHAITE; -.
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; 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:SF2; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE AGS1; 1.
DR   PANTHER; PTHR47182; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE AGS1-RELATED; 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:UP000005240};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1194..1217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1898..1918
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1938..1955
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1982..1997
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2017..2038
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2045..2068
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2088..2108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2115..2134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2168..2188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          196..656
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          26..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1650..1715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2211 AA;  247041 MW;  6989D9E9BA4746DE CRC64;
     MYLLDTFGFD FQPGYNYEPC GPSVFPKLSR TSGGPETKVI SEPEEQGEPE EQGEPEEQGE
     RWSIRCQKTC PIPKRAQSRP TLSVQTFLKT DLGKVQLEYW HNLVNLFNSS PLPTHLTGSP
     SSPIAQSASW LAPPIEGLSG DYPLPYLKEF QPASTPGRQD GSSVPTDYYS DWPEKSQNGS
     RYTPSPANWR ELPIYTVILD RFMDGNPSNN DFYKSRSEWD FLSNQLRHGG DIEGFAQDRV
     LDYIYGMGYR TIYIAGTPWL NMPWQSDGYS ALDFTLLDPH FGTLSEWRAA IDKIHSKGMY
     VMLDTTTTTL SDFLEFKGNS GGAAPFNLHG YEVEYKTTVQ KPWNINQYAE FKFTNSRDQS
     CRLPKFYNPN GTDVLPPTDW DGCYAGDFNQ FGDSSPAGKA PGWQDQLTKY SGVQDRLRDW
     DSGVAAKLEK LACMTVKALD MDALRVDKAT QQTLEFMGKW GGSLRTCAKD LGKNNFFITG
     EISDGNTFGS LYIGRGRQPA HYANLEFDTA ALVTANQTEN FMRPIGENAL DSAAFHYSIY
     RSLTRFLGMD GELDSPYDIP VNWVEAWRQI FVTNDLFNQE TQQLDPRHLY GTTNQDNFRW
     ASLINGTERF LLGQLVTNLI MPGIPFAFYG EEQDLHIFDS QANDYLYGRQ PMSSSKAWQT
     HGCYKLGSKK YPTMPLGKAL NGCKDDWNSL DHYDPTSNTR NMLAHFAYLR SQYASLQDGF
     NLTQLGNWTH FGELPASSHT PTEWGLWSVS RSSLKSQNLS GPNSQLPVWI LYSNVNQTTT
     FSYDCSSKLA ITSPYPGPST VRNLFYPYET YDLDPSSTSS TWDDAPPFLG CLKSITMDPL
     SYKVLVPASN WVSPQPRLVG FVPGHDARIL SQADNDNETI PISLSFSDEL SCEGVSSSLS
     LSYTIDPNSK ASPRIDLEHA NCSKIESPSN STQSALPAVW QWSASIVGAA DGIYELILNN
     ATGQNGIHTN SIDHLLLRKG RKLNPITFSD VSYSESLLEN KDGKYTLRSD APGADMMRYS
     VDFGKTYSNW TRYSSELTLP DNAFSISKFW DGDHVRVQYW SRLTGSAAPT IDADINFDGG
     FKRRFPQLIL RGAYNKWGFD EGIPGLLSPR SENMTIDVIT SWPHEFQLAV FEARDKVFYG
     DVDNDGVLDL LPPNSQARNF LSLPPPSKPY LGWRIMINPR DLTWGAQPVG HQKIVIMLLF
     LLLFIPPTTA LLACWLYQRI FYKIKHNQHL PKSMLNSQIP STLKHAITPQ LGSKKETPHF
     SFANTWPENI NSRRKVLIAT LEYEIIDWGI KVKIGGWETP DLTIYHINDY HGALAPLYLL
     PKIIPVALSL HNAEFQGQWP LGTPEEENEV CQSFNISSKV CSKYARYGSV FNLLHSAASY
     ISHHQKSVGV AGVSEKYGKR SWARYPVLWT LKSIEPLPNP DPTDVESLDV TPPDMRRIQI
     DQEAEAKRPG NKLKLQDTSF VFVGRWSFQK GVDLIADVFP LLLETRKDVQ LVAIGPVIDL
     YGKLAALKLN RLMESYPDRV YSKPEFTALP DFVFSGGDFA LIPSRDEPFG LVAVEFGRKG
     ALGVGSRLGG LGLMPGWWFP VESDSTAHLH SQFAKTLNAA LECPEEERAV LRARSVHQRF
     PVLEWRMKME DIHSRSVKAS RKYAGRLTMN INQNEVLKPD ESSSASHDQG NPRQAHPSAT
     ESNKPGQICT SSTGNQSNTF GSHLNPTRPS SDVSRILSSS NQLAVQLSEA VKRLIITKNR
     SSTPPSRLSG RITDKASVDG AITPSGRPQN NDQEILTSVV TLDKNNGNAG EHNPADFQRT
     YCGQDDRNSP LNQGVKDFTD EDGKASQEFV HKTAETGLRL AGLHSLLAIG QILGATSFQL
     SLLSGTSSNG SFDFYAFIFI GLPSLSENLK QYSRRHSLAV AASGFYSFAS SAGFLFFSSN
     FGEEAGGTTD SWVRRACIVQ GTQQVWVGAL WYWGFKLQNP KYYRNVPGTV PNFTRALFRR
     KLVLWYLAAE ILRNYWLSGP YGRNWNFLWT RETSFGVTLF LLLFFFVGVW GVTIWGLSRA
     SKSHTWIVAI FAIGLGAPRW CQMLWGTSSV ASYISWGGSA GSHIATSLWL WLGVLDAVQG
     VGLGMILLQT LSRVHVAATL CLAQIIGSTA VLVARATAPD RIGPGGVFPD LALWNPKFSY
     LDSPLANWQF WIALICQLII VTGYFVLFRR EIPKGLFQLT SSYSLQQLSK P
//
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