ID A0A180GL30_PUCT1 Unreviewed; 2391 AA.
AC A0A180GL30;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=PTTG_08732 {ECO:0000313|EMBL:OAV93335.1};
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|EMBL:OAV93335.1};
RN [1] {ECO:0000313|EMBL:OAV93335.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV93335.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAV93335.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV93335.1};
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.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAV93335.1}.
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DR EMBL; ADAS02000052; OAV93335.1; -; Genomic_DNA.
DR STRING; 630390.A0A180GL30; -.
DR VEuPathDB; FungiDB:PTTG_08732; -.
DR OrthoDB; 141134at2759; -.
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; 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}; 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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..2391
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008110019"
FT TRANSMEM 1091..1114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1961..1984
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1996..2015
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2027..2045
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2057..2079
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2091..2111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2131..2151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2172..2191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2211..2232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2241..2263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2283..2303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2310..2329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2363..2383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..553
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1674..1731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1762..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1763..1797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2391 AA; 267334 MW; EA36E8E2F7A6B5E0 CRC64;
MATTMIPSRT RLMNLTVLLF GLLHLSLIHS YPYDPAFSDY NININSSAGN NILDYYSDWP
EKSHNGSRYT PSPANWRELP IYTVILDRRA FVFLANGAFM DGNPSNNDFY KSRSEWDFLS
NQLRHGGDIE GFAQDRVLDY IYGMGYRTIY IAGTPWLNMP WQSDGYSALD FTLLDPHFGT
LSEWRAAIDK IHSKGMYVML DTTTTTLSDF LEFKGNSGKA APFNLHGYEV EYKTTVQKPW
NINQYAEFQF TNSRDQSCRL PKFYNPNGTD VLPPADWDGC YAGDFNQFGD SSPAGKAPGW
QDQLTKYSGV QDRLRDWDSG VAAKLEKLAC MTVKALDMDA LRVDKATQQT LEFMGKWGGA
LRTCAKDLGK NNFFITGEIS DGNTFGSLYI GRGRQPAHYA NLQFDTAALV TANQTENFMR
PVGENALDSA AFHYSIYRSL TRFLGMDGEL DSPYDIPVNW VEAWREIFVT NDLLNQETQQ
LDPRHLYGTT NQDNFRWASL INGTERFLLG QLVTNLIMPG IPFAFYGEEQ DLHIFDSQAN
DYLYGRQPMS SSKAWQAHGC YKLGSKKYPT MPLGKALNGC KDDWNSLDHY DPTSNTRNML
GHFAYLRSQY SSLQDGFNLT QLGNWTTFGE LPASSHTPTE WGLWSVSRSP LKSQKLSGPN
PELPVWILYS NVNQTTTFSY DCASKLAITS PYPAPSTVRN LFYPYETYDL DPSSTSSTWD
EAPPFLGCLK SITMEPLSYK ALVPASNWTP PQPRLVGFTP GHDARILSQA DNDNETIPIS
FSFSDELLCE GVSSSLSLSY TIDPNSKASP RIDLEHANCS KIESSSNSTQ NALPAVWQWS
ASIVGAADGI YELVLNNATG QNGIHTNSID HLLLRKGRKQ NPITFSDVSY PESLLESKDG
KYTLRSDAPG ADLMRYSIDF GKTYSNWTRY SSELTLPDNA FSISKFWEGD HVRVQYWSRL
AGSAAAAIDA DINFAGGYKR KFPQLILRGA YNKWGFDEGI PGLLSPRSEN MTIDVITSWP
HEFQLAVFEA REKVFYGDVD NDGVLDLLPP NSQARNFLSL PPPSKPYLGW RIMINPKDLT
WGAQPVGHQK IVIMLLILFL FIPPTTALLA CWLYQRIFYK VKHNQYGFQT AGLNSFLPIQ
HLPKSMRNSR IPSTLKHVIT PHFGSNAEKS QASFANTWPD NAGSRRKVLI ATLEYEIIDW
GIKVKIGGLG VMTSLMGKVM EDLDLLWVIP KVSGLEYPEA ERAEPIAVVV FGETYLVELQ
IHKFKNITYF LLDSPIFRAN SKINPYPARM DDLDSAIFYS YWNQSIAEIC RRTPDLTIYH
INDYHGALAP LYLLPKIIPV SLSLHNAEFQ GQWPLGTPEE ENEVCRSFNI SSKVCSKYAR
YGSVFNLLHS AASYISHHQN SVGVAGVSEK YGKRSWARYP VLWTLKSIEP LPNPDPTDVE
SLDVTPPDMR RIQIDQEAEA ERPGNKLKLQ EWAGLHEDPK AQVFVFVGRW SFQKGVDLIA
DVFPLFLEKH KDVQLVAIGP VIDLYGKLAA LKLNRLMESY PGRVYSKPEF TALPDFVFSG
GDFALIPSRD EPFGLVAVEF GRKGALGVGS RLGGLGLMPG WWFPVESDST AHLHSQFAKT
LRAALECPEE ERAVLRARSV HQRFPVLEWR IKMEDIHARS VRASRKYAGR LTMNTNPTEV
IKSDESSSVS HDQGKPVQVH PPSSESNKTG VICTPSTKNP TNTFGSQLNH TRPSLDVSRM
LSSSHQLAVQ LSEAVKRLII TKRGSSTHPS RPSEQRTESA PLDGAVTPSE RPQNNDQEIL
TSTIITLDKN NGNTGEHNPA DFQRTYCGQD DKNSPLNQGL KDFTDEDGKA SQEFVRRLQK
LDASNSRSEL CIARYIVAAH KEHFNQVRKG TLALARTRYA SSPTLSVTSI IPRTMLGGGI
SSPTNGLHDI SDQVKNEKSD TLDVTAALSM NLWQIRLQRR VFGWPIYTIL LAIGQILGAT
SFQLSLLSGT SSNGSFDFYV IGAVNILGSA SWYGLSRRKP STWSLSLPWI FFGLAFIFIG
LPSLSDNLKQ YSRRHPLAVA ASGFYSFASS AGFLFFSSNF GEEAGGTTDS WVRRACIVQG
TQQVWVGALW YWGFKLQNVD PTNAALAPPG WINAITLSLG AGCFFIAYIL FTGLPKYYRN
VPGTVPNFTR ALFRRKLVLW YLAAEILRNY WLSGPYGRNW NFLWTRETSF GITLFLLLFF
FVGVWGAAIW GLSRASKSHT WIVAIFAIGL GAPRWCQMLW GTSSVASYIS WGGSAGSHIA
TSLWLWLGVL DAVQGVGLGM ILLQTLSRVH VAATLCLAQI IGSTAVLVAR ATAPDRIGPG
GVFPDLALWN PKFSYLDSPL ANWQFWIALI CQLIIVTGYF VLFRREQLSK P
//
