ID J4G7G3_9APHY Unreviewed; 2350 AA.
AC J4G7G3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=FIBRA_04479 {ECO:0000313|EMBL:CCM02383.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM02383.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM02383.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM02383.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(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; HE797078; CCM02383.1; -; Genomic_DNA.
DR RefSeq; XP_012181666.1; XM_012326276.1.
DR STRING; 599839.J4G7G3; -.
DR GeneID; 24097294; -.
DR HOGENOM; CLU_000488_0_0_1; -.
DR InParanoid; J4G7G3; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000006352; 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 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352};
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..2350
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003778398"
FT TRANSMEM 1059..1085
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1925..1948
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1960..1979
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1986..2005
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2025..2042
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2054..2075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2087..2110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2170..2189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2274..2292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2322..2341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..519
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1664..1705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2350 AA; 263636 MW; A86EE1A862011947 CRC64;
MWALAALGSL LSLAPLVFAS PYREDLVAYN VNTNKTATNV LDYYYPQRAN YTPSPDNWRA
LPFYTILLDK FADGDPTNND FFGSVYEWDW RETQLRAGGD LKGMLARLDY LQGMGVKAIY
TSGTPWLNMI WEADSYSPLD FSVIDPHYGT LQDWQNAIDE IHSRGMYIML DFTVGTMSNI
VGFKGFENVS APFNIQEYDA AWLDPQYQPW GFETYADFQF NNTYNTSCEM PVFWGDAGTI
VDIGWNGGCY ASEFDQYGDM EAFGVHPDWQ RQLSKFASVQ DRLREWRPDV MAKLTKFSCM
ALTALDFDAI RIDKSTQMTV QGLVDWTSTT RQCAIELGKK NFLITGEVTG GDYFGSLYYG
RGRTPTERPP GFLQAANVTQ SEDQYFLRDI SQDGLDGAAF HYSIYRGLTR FLGMDGDLED
AYDVSNNFVT AWNEMFVNED MINPNTGLVD PRHLYGTSNF DVFRWPTLDN GTERSVLGAF
MAYLVMPGIS LMYYGEEQNF YIYDNTASNY LYGRQAMFSN TAWQRHGCYS LGSSQYYNIP
MGRALIACKD DWNSLDHFDP TSDTRRLFSQ FLYLRTVYAA LQDGFNLVQR GNWTYDIARP
GSNGTLTEMG LWSVSRSAIE GYQTLTGNNT GQVWLLYANN NITTTWSHDC MKSLWISSPY
ESGMTVRSLF HPYETYVLEQ SGSPYYNNGT GPYYGCLGNI TLPPYGFKVL VPVDQWVPPP
PAITRFLPGH DARITSNPNN MTINITLEFN LEMDCNGVTE AITLNMSSAG NITTPTIDKS
TVQCNAVTEP QPAQVQGVSL STWAWSATIQ DVPDGIMEIV VKNPSTSDGS ASTNSIDHLL
VRKGQPNNIM VFPTYNYDTD GFQYSNGQYS YTHKAYGADM FRYSWNFAQN WSDWRSWEDV
TTIPADVFDT SDNWWEGQHL MVQYWSYLAQ TSSVVIHADH DYSIPRRVPQ FLVRGIYNQW
GIDKGLPYAM SQNSNGLWEL EIMATWPSYV QLCVFGFDNY FYGDVDGDGV LDRLPPNTLS
PNYLNMSAPP RPHLAWNLVV DDATLTWWVE PVGQSAVGAI FFALLLAIPF ITGAIAVAVF
MWSFYGIKYN KWGVKPNKDH NYFPIVGTFG SKSKASIHEA HTPLSEKVFG PKHHADIIGW
PEDKNKRRKV LISTLEYEII DWKLKVKIGG LGVMSSLMGK AMTDVDLIWV VPKVKDLEYP
PGEPCEPIEV VIFGEPYLIE VETHVLDNIT YVILDSPVFR AQTKADPYPA RMDDLSSAIF
YSTWNQAIAA TVRRYPDIDI YHINDYHGAL VPIYLLPKVL PICLSLHNAE FQGLWPLRTK
EEMKEVCSAF NISKEHCTKY VQFGNTFNLL HAAASFISVH QKSVGVAGVS DKYGKRSWAR
YPALWTLKHV DSLPNPDPTD IAALDENPVD VKSVQIDQVA EAERPEHKRQ AQEWAGIKQD
PNADLFVFVG RWSKQKGVDL IADVMPSLLE KRSSIQLITV GPVIDLYGRF AAEKLARLME
LYPDRVFSKP EFTALPPYLF SGADFALIPS RDEPFGLVAV EFGRKGALGV GSRLGGLGLM
PGWWFPVEST STEHMMSQLT KTIKMALKSS QEERAMLRAR SAVQRFPVVE WRQRMEDFHR
RSINMSRDVA GPNAWRSADA LVGESGIAVA EADDWEPGHV AFPSQPDWEI RSVNGSPGAG
TPGTPGSPGR WSQETLTLGP DGSMAMRPRL IQESRRVSYA TDLSENDSDY FSNAHQPSSH
DSGPDFGNFL ERANRTIAQD QRNVPDPFLD PSSSKPFGSH SRISSIESIA SIVDEKYNSP
LNKAIASFTD ADGGVAQEFV QKLQMLNSHN SKGELSIEKF LTKSEEAFFD KVKRERLSSA
ASIRSSRRES IWGTPAPSSF EYSRPPSLNH FLGADAIPMS DYGGPPNEKD VVIMSSLQIA
MSREIFGWPL YGIVIGIGQM LSATTFQLTL LSGANTQSNL QLYVLGGIFL AASAVWYPLF
RLKPSVYVLS APWLFFGVAF FLIGLPSVTP SLYSTHYALS SAATWSYAVA SAAAFLFFGL
NFGEEAGAAT DTWIMRACIV QGSQQIWVAA LWYWGYTLDD APAGNMAPWW IVLIVWPLAV
MSVIFAYLML YGLPDYYRQT PPKVPHFLKT LFRRKIVLWF LGSEILRDYW LSGPYGRNWT
FLWNVDIPKW QILLLVVAFF IGVWGLLMLG LTRLSKTHTW LLPVFAVGLG APRWCQMMWG
TSSLALYIPW AGNAGPYLGV SLWLWLGVLD AIQGVGLGMI LLQTLSRLHV CATLAFAQII
GSVCVIVARA TAPDTIGPES VFPDAAAWSF SDGLKGSPMA SAPFWIALVC QIAIVVGYFW
FYRKEQLSRP
//
