ID A0A0D2GFK6_9EURO Unreviewed; 2538 AA.
AC A0A0D2GFK6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=PV04_03191 {ECO:0000313|EMBL:KIW70964.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW70964.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW70964.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW70964.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN846957; KIW70964.1; -; Genomic_DNA.
DR STRING; 5601.A0A0D2GFK6; -.
DR HOGENOM; CLU_000488_0_0_1; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000054266; 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 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; 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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2147..2165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2172..2194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2206..2226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2238..2261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2281..2308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2328..2345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2365..2385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2392..2412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2437..2458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2465..2487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2507..2527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 148..604
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1790..1961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2048..2082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1799..1817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1867..1890
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1928..1945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2050..2082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2538 AA; 284229 MW; C7F3C77654056227 CRC64;
MLSSVPACPQ RDPLSERKTH GVRGRLTFVE GFSTLRCEIF PTYSLYTFRC LHHFGLRKSP
RSNTLASTIT ITLNQSFVFY LHTMWFYTLV SSVFLFLSSC GALRYDPAFA QYNLNQNQTA
INPLDYWGEW TGHQYHPSPS NWRFPFYTLF LDRFVNGDPS NDNINGTAYE HDLNSNQMRH
GGDLQGLVDT LDYLHGMGIK GIYIAGSPFI NSPWGYDQYS PLDLSVLDQH FGTINMWRSA
VEEMHARGMY VILDNTFATL GDLIGFEGYL NTTTPFTLKE HNVQWKSSRE YHDFHIGNNY
NKTCQYPKFW LETGYPVGED VTSQMVGCYD SDFDQYGDTE AFGVFPDWRR ELSKFASVQD
RLREWHEPVR LKLENFYCMM IAQLDIDGYR YDKATQSTVD AMGYMNDAMR RCARRFGKDN
FFTPGEITGG NVFGALFLGR GRQPDMLPEN LTVAATMTDR SPAKYFLRDG AHGALDAAAF
HYTVYRTLTR FLGMDGNLEA GYDAPRNFVD MWNTFLLTND FVNPNTGKVD PRHMYGVTNQ
DVFRWPAITN GVERQLLGHF ITTLHMPGAP LLLWGEEQAF YVLDNTASNY IFGRQAMSSA
TAWQTHGCYH LSSTQFFGIP LNASRHGCQD ETVSYDHRDP AHPVRNIIHH MNQLREQYPV
LQDGFFLQQL SNQTEEIQYP GSGNVTTETG MWSVMRSGFP GVQDLGDTGA GDLPVWLLYS
NANVSTTYTF DCNDNATALN TTSLISPYDA GTVVKNLFNP YDEHTLGSSV HRLGINGSTN
PNGCLSSLDM AAYDFRAYVP KDQWVGPKPM ITKFTPGHDA RLKSTVNAGG TESVNVEFQF
SVEMDCDSVT NSILFNSSTE SAATPSIDRS SITCANLDQP QTPAYVGAIS STWSWSAKLD
NVANGIHSIS VRNASSVAGD VTNAVDHFLF RIGRTDNPMV FTGAANYSSS LLSKSDNGSL
IISHNAAGAD KWRYSTNWGS SFSDWMPYRG GKTQIEKQAW SGTKLQAWKG DHVRVEYFSR
LAGSSDHIQE GDVDFSTPRR FPHLFLNGPY NQYGYDAGLN NEMKLTDNST WDHHFMTEWS
LSGTLAQINV WGLNPDGKPD QTIVMGDADG DSILDRLPPS SLSSVVLNIT QPPPKPYLGW
RLVINDGNLR FELRPSGNMW PQLILYVLLW TVPVITATFG VWSFMQSFYQ IKFNEVGISE
KKSFVPAVFK SKFKKLPDEE NSPGVLTKFS RKPKFLQPTG ALIDQQKRRT VLIATMEYDI
EDWAIKIKIG GLGVMAQLMG KNLGHQDLIW VVPCVGGVDY PEDQKADPMT VTVLGKPYEV
QVQYHVLRNI TYVLLDSPVF RQQTKSEPYP PRMDDLSSAI YYSAWNQCIA QALNRFPVDI
YHINDYHGSV APLYLLPRTI PACLSLHNAE FQGLWPMRTN QERDEVCSVF NLSSEIVAKY
VQFGEVFNLL HAGASYLRVH QRGFGAVGVS KKYGKRSYAR YPIFWGLKKV GKLPNPDPSD
TGEWDKKLPK ESDIFVDPEF EAARPELKRQ AQEWAGLEQN PKAELFVFVG RWSMQKGVDL
IADVFPSILE SNPNVQLITI GPVIDLYGKF AAMKLDRMMQ LYPGRVFSKP VFTALPPFIF
SGAEFALIPS RDEPFGLVAV EFGRKGALGV GARVGGLGQM PGWWYTVESM TTAHLLHQFK
QAINEALGSS TEIRALMRAR SAKQRFPVAQ WVEDLEILQS TAIRIHDKLE ATRRHTAAAD
LIGTSAWNTP FASGTATPSG LRTPIFGHSR MSSYTTLQSL TARLRNLGHS REVSQETYRR
PNSSHSHTPS GLSRSASLGS RRGPGHVDVQ DEHDGDEPRT PSLLPPIPDV GGDDTGLRAG
STQNPNEYLD DEDEDLASEF EDDDDDDDDV VTMPKQTSGR YERIPLNDDS PRTPPSSSYR
PSRPAGLELT RLSNSPYSRR NSLDQPRPDS GLLIPPPVLT DNNRVSSTPS LLSMNSIVGE
KTDFKLQQVD PFFTDSNGEF ARSFGKKLED LTGHNSESTT CIEEFLVKSE KQWFNTFRDV
KLGRHTAIPS GRNSMHTNRE SRTTSAAPSI YGGNTDADSH PDPNNLAEQF LLGENYKPPT
GLRKWMQVRA GDWPVYAYFM GFGQIIAANS YQITLLTGEV GQTATKLYSI ASIYLATSIC
WWLLFRRFQS RLCLSLPFFF YGLAFLLIGT AHYGSSISSR GWIQDVGTGM YAVASSSGSI
FFALNFGDEG GAQVKAWVFR ACVIQGTQQI YVVALWYWGA YLNKRTVTQL VSTLNPITDT
WKITAITLPI AFLLWVIGLL MWLGLPSYYR QAPGQMPSFY KSLTRRKIVL WFFVTVIIQN
FFLSAPYGRN WSFLWSSSHA KNWQVVLLVA FFFIGVWAGA LWLFATLSKS HSWILPLFAI
GLGAPRWAQI WWGTSNIGAY LPWAGGYTAS ALASRALWLW LGTLDALQGV GLGMILLATL
TRVHVAFTLI TAQVLGSLAT IVARACAPNK IGPGPISPDI SGGVSNVWQA WFWIGLVFNL
AICAGYFKFY RSEQLSKP
//
