ID G7XVV7_ASPKW Unreviewed; 2397 AA.
AC G7XVV7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=AKAW_09180 {ECO:0000313|EMBL:GAA91066.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA91066.1};
RN [1] {ECO:0000313|EMBL:GAA91066.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA91066.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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; DF126477; GAA91066.1; -; Genomic_DNA.
DR STRING; 1033177.G7XVV7; -.
DR VEuPathDB; FungiDB:AKAW_09180; -.
DR eggNOG; ENOG502QQX3; Eukaryota.
DR InParanoid; G7XVV7; -.
DR Proteomes; UP000006812; 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; cd11323; AmyAc_AGS; 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; 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; PF13692; Glyco_trans_1_4; 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}; 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..2397
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003505914"
FT TRANSMEM 1070..1095
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1975..1995
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2007..2026
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2038..2056
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2068..2088
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2100..2120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2140..2167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2187..2204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2224..2243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2250..2267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2279..2303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2324..2346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2369..2389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..536
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1693..1757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1918..1943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1693..1712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1924..1940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2397 AA; 269498 MW; C961C3D3179BC36E CRC64;
MFGTTVQRCV VLILGLLSVT TVGWPYDESL VDYNLNENKT AEGPINYWGE WPNHTYHPSP
DNWRFPIYTI FLDRIANGDP ANDDINGTTY EHVLDSNQMR HGGDLVGLID TLDYIRGMGF
KGIYFAGTGL MNLPWGYDGY SPVDTTLLDK HHGTLSDWRR TIKEIHDRDM YVIMDNTLAT
LSNLIGFKGH LNDSADFNAK EYEVEYVTER QYADFKFGND YNDTCNYPRF WNETGYPLTS
GGVQDLKGCY NSDFDQYGEL EAFGNFPDWK RQLTKFASVQ DRLREWHKPV RDVITRHSCI
VIASLDIDGF RFDKAVQATL DPLGDMLAVY RECAKQYGKK NFFLPGEITS GNTFGSLYLG
RGRQPNQTPD SADAGAKLTN ASSDSYFLRD DGLQALDAAA FHYTIYRSMT RFLGMDGNLV
AGFDLPTDFI EAWNGMLVTN DFINAFTGEL DPRHMYGVSN QDNFRWPAIK NGTEKYLLGL
YIVTLELPGI PLVLWGEEQE MYVFDATASN YLFGRQPMTY QTAWWTHGCF SLNTSKFYDF
PNDKGLNGCN DITVTYDQRN PAHPLRNIMK RMFEIREHYP VANDGFNLQT IAQLTQDLYL
PGSSTTPTVT GLWSVLRSYY PGVQKEASTS NDTLWLVYHN ANKTETYGQN CSSKDSALLS
PFESGTKLKN LFYPYDELTL QDGPSDASNG TESYGCTTKM KLLPWEFRAY VKASDFVEPG
PTVTEFVPGH DARLLSSEDT GETLEIQLGY SKTMDCSAIT KAISLNSTTI KGVNASLDTS
SVSCTNVTAR TSSNNYVGEV PTVWTWSANL TNVYHGIHQI TVKNASTTSG TRVDAIDRFL
FRVGTHTNPL ISPLANYSTS LVHKSDNGSY YVQHDAAGAD QFRYTTDFGR SWSNWTDYTG
GNTTIDFPTW TGTDAQKWKG THIRVQYFSR LTGSSDYIQE GDYDWESDVP RRFPHLWWNG
PYNQYGYDAG LDSKMRFDTK DRRWKYDFVY EWPSVGQISV WGTGKDGVPE TTNVYGDVDN
SSVVQVLPPS YLSSNVINIT ELPPFPHLGW TISLNDANLR YELLPVGSGW AQLVLFILLW
VVPILMGLAG VFIFIRTFYR VELNTDGNVV KEDKLPLLFW RRMKGQAGGD GQMDREESEV
AAVAGDLAIA GAPEKRRTVL IATMEYDIAD WQAKVKIGGL GVMAQLMSQN LGYQNLIWVV
PCVGDIEYPE DTPTEPYVVK ILDNPYLVNV QYHVLNNITY VLLDAPVFRQ QTKAEPYPPR
MDDLDSAIYY SAWNQCIAET IKRFPSIDMY HINDFHGCLA PLYLLPTRTI PVCLSLHNAE
FQGLWPLRTQ QEKKEVCSVF NLPVEVATKY CQFGNVFNLL HTGASYLRFH QRGFGAVGVS
KKYGKRSWAR YPIFWSLDKI GSLPNPDPTD TAALEDTPDE KALTRSYEER ITDKLEAQKW
AGLTEDPKAD LLVFVGRWSK QKGVDLIADV IPAVLSDRPQ VQVICVGPII DLYGRLAAIK
LEKIAAMFPG RVFSRPEFTA LPPCVFSGAD FALIPSRDEP FGLIAVEFGR KGALGIGSRI
GGLGQMPGWW YTVESDATRH LLHQLRTAIK SALDSSPETR AQMRANSAKQ RFPVLEWIQK
LETLQRTSIK IHHEKNKDTV TGSIPESESV WDLQNLQSAR YSTVALPNMA LSRSDGSDTP
PEAMIQQAHA RLQEIQASEG SSRDSSLNRK LSLGRRSGPG QGRKRLTKKQ ATASQISTDH
GEDEHDTDAD EDDHRPQEDY ISPEEAMQAV NNTLSPHAIT GDSTPRASYL SRPVSPYPVS
QISTPACPTP PPMTHFRTVS MLSLPSVVGD HNRLSSLGGE DKDQPVFELQ KVDPTFTDSL
GHFTRRFEQS LDKLNKKNSI TDYCIEVYLM KSERKFYNSY NDAQLKKQPK DRGIAIPSSV
SVVHDGPGTD NRQSYSSEDS EQLNGEDEID RWLMRLGYTR PIAVQRFMRR RLGNWPVYSL
FLGLGQIIAT NSAQITLLVG QVGETAVKLY VIAAIYCLSS IAWWFMYHRF PAVISLSLPW
FIYCLAFIVI GVSPFGLTSL GRSWAQNVAA GVYAIASSSG SLFFALNFGD QGAVPVKDWM
FRASIIQGIS QIYTVALWFW SSKVTAAEVG GVSVAALSSW RLTAVVMPIA ALCFVIGVLL
ALGLPNYYRQ APSRILFFYK SLFRRRIILW FFFMVIVQNW FLSAAFGRNW SFLWTSKHVK
PWEIVLLVFG FFVVLWVAIL VIFRALSKEH SWILPVFGLS LGAPRWAQTW WGTSNIGYYL
PWAGSLVSGS IVTRCLWLWL GLLDEIQQVG LGMILLQTMT RVHVCFVLLA AQALGSIATI
CARGFAPNKI GPGDISPDVG TSVDKVGNAW FWIALFFQLL ASWGFLLFYR REQLNRP
//
