ID A0A094CIH0_9PEZI Unreviewed; 2470 AA.
AC A0A094CIH0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=V497_08274 {ECO:0000313|EMBL:KFY53764.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY53764.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY53764.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY53764.1}.
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DR EMBL; JPJZ01001227; KFY53764.1; -; Genomic_DNA.
DR STRING; 1420910.A0A094CIH0; -.
DR HOGENOM; CLU_000488_0_0_1; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000029268; 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; 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:UP000029268};
KW 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..2470
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001893975"
FT TRANSMEM 1155..1181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2043..2063
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2075..2093
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2100..2120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2132..2155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2167..2188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2214..2236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2257..2273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2293..2316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2328..2356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2368..2388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2395..2414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2443..2462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..523
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 710..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1725..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1804..1879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1959..2005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1852..1867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2470 AA; 273058 MW; EE7D8EB061DCC792 CRC64;
MASLLRIALW GLYALGSNAL RFEQEYVGYN LNEDDPNLGA VNNKWAGHTY HPSPTNWRFP
FYTLFLDKFV NGDPANDNIN GTLFEHDTMQ TLLRHGGDIQ GLIDSLDYIA GMGVKGLYIA
GTPWLNFPWG ADSYSPLDFT LLDQHYGDIT KYREMVDEIH RRGMYIIVDT TMSTMGDLHG
FEGHLNDSAP FKPTEYKVIL RDKTRQYHDF HPQTEDIYNE TCAYPTFWDE TGHEVGEDVL
SQLGGCFDSE FDQAGDIPGV GFFPDWQNQL GKYQSVQDRL REWMPSVREK LENFACLTIQ
KLDIDGYRFD KGTQITLDAL ADINLSIREC AREVGKDNFF ITGEISGGNT FGSLYLGRGR
TPEQYGNITL DEAVKLNNAS NATLFMRDED HGAYDAAAFH YSVYRSLTRF LGMQGFDSSF
FDVPADWVET WNVLLRSNDL VNPNTNKLDP RHMYGTANQD VFRWPAIQDG VEKQLLGSFI
TTIHMPGIPL MYYGEEQGLY VLDNTADNYL FGRQAMSASV AWQAHGCYNL SSSQYRDFGD
VNAQKACEDN SVSLDHRDPS HPIRNIIKGM HQMRTNYPVL NDGLFLQSLS NKTKQVPIDK
DTREVGLWSA LRSELPKLQD LSTAGGQGKQ EVWLLYHNDN HTGNYEFDCA DEELALVAPF
PPGTVVRNLF SPYDEVTLLD GIVVPGFGSL DFTAAAVEAR QVLPADPVET AADTAAETAA
ETAAKTAAEP AATDVPTGTD KVKSSTETGT GKKASTTGKP KSTKTSAKPK ATTSAPPPKF
TSGCLKKVSL KPYEFRAYVP STKWVAPNPM ITRFVPGHDA RLKSTVPLGQ QENIDIALYF
SNEMSCTSVT KGITITSTTE DATTASILEG SIKCATVPAQ VELNVPGNIP STWKFSATLT
GVGHGVHSIT VKDVAAEAGD TSTGSTDKFI FRTGAEDNPI TFPRSANYSS SLLKRRDNGT
LYISHKAAGA DLWRYTLDWT HYSQWFTYEG GEANLPPKNW TGTAKQKWKG EHVIVEYYNK
DSGSSDYVQH GDLDSPPRRF PNLFALGTFN GFGADSGILN TFRLDKDGWW TYDLISEWPG
QLQLNQWGIN PDGLPDQTAV YGDIDNDQVL DRTPPPSLRL ASFDLKDAPP MPHLGYRLSV
NDGTLAYTIL PTGNMWFQIV VFVVSTVAPV LTGLFAVWGF MGAFYSVKFN KVGVKVKGMG
AFVPAFIGKR FAGKEKSRAL IPGSAAASRL SLVPGAAGAA AGALADRRTI LIATMEYDIE
DWAIKIKIGG LGVMAQLMGK NLGHQDLIWV VPCVGGVEYP EAERAEPMSV TILGSTYEVE
VQYHILRNIT YVLLDAPVFR KQTKTDPYPA RMDDLESAVY YSTWNQCIAL AIARFPIDLY
HINDYHGAAA PLYMLPDRTI PVCLSLHNAE FQGLWPLRNS KEFNEVCSVF NLPAEIVERY
VQFGDVFNLL HAGASYIRLH QKGFGAVGVS AKYGARSHAR YPIFWGLKKI GQLPNPDPTD
LGEWTGKQDD SKVVIDETFE SARPGLKGQA QEWAGLNQDP DAELFVFVGR WSMQKGIDLI
ADVFPAVLES NPKVQLLTVG PVIDLYGKFA ALKLDVMMKK YPGRVYSKPE FTALPPFIFS
GAEFALIPSR DEPFGLVAVE FGRKGALGVG ARVGGLGQMP GWWFTVESTT TAHMLSQFKG
SIKEALASKL ETRRKMRARS AKQRFPVAAW VDQLEKLQSS AINTHVKEVE RGGPRSGLSL
PLPGRRSRGN SGTYSRPVSG MYSRTMSENA TPSGGNSPPL HPVYFNSDNS MPSTAAASQI
TLNQSDFDRR RSPLDMGDDD NDLGDGLDRE SLISDPSKPV SLLSRDIPTP PEAEDGPSRE
GDDLLGNQAR GRDGLGIHYQ SRSRPVSMLS LNTVVGDKKD FLLQKVDPDF TDSKGEYYKA
FEGKLANLSA GNSEDALCIE DYLVKSEREW YSDFKNAKLG RSSDRSRSGS RSRSRSRSRS
RGRSDSGSSV LTKKNRASPT PVLYDGEHEA YNMGDDDDEW LLGQDYKPPT GVRYLMQRRI
GDWPVYSFVL AFGQIMAANS YQVTLLSGTA SSASIVYATG AIYIAFSVVW WILFRKAPSV
YVLSVPFIFY GSAFFLLGLV PVANSSKVAQ LWIENVATGL YAAASPSGSI FFALNFGDEG
GSPIKSWVFR ACIIQGTQQI YVVALWAWGN YQNNITGTGA ALSDSMITTT SLKFTAIMVP
IACLIWAIGA LCYFGLPSYY RQAPGHVPSF YKAIMRRNIV IWFFIVIIIQ NYFLSASTGR
NWQYLWSSQA AQIYQIALLA IFFFIIVWAL LLLLFAKLSQ AHSWILPLFA IGLIAPRWAQ
ILWATSNIGI LLPWTGSPLA SALVSRSLWL WLGVLDAFQG VGFGMILLQT LTRLHIAYTL
VGAQIFGSVA TMIARATSPN RDGQGDLFPD FSVGPLPGLS KPWFWVGLAF QLIITLGFLR
FFRKEQLSKP
//