ID G0S3E0_CHATD Unreviewed; 2372 AA.
AC G0S3E0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=CTHT_0020670 {ECO:0000313|EMBL:EGS22523.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS22523.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL988040; EGS22523.1; -; Genomic_DNA.
DR RefSeq; XP_006692542.1; XM_006692479.1.
DR STRING; 759272.G0S3E0; -.
DR GeneID; 18256105; -.
DR KEGG; cthr:CTHT_0020670; -.
DR eggNOG; ENOG502QQX3; Eukaryota.
DR HOGENOM; CLU_000488_0_0_1; -.
DR OMA; TKADPYI; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000008066; 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:UP000008066};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..2372
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003409272"
FT TRANSMEM 1079..1101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1948..1970
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1982..1999
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2006..2028
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2040..2060
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2072..2093
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2113..2136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2157..2176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2196..2217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2224..2241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2253..2277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2298..2316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2345..2364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..523
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1652..1745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1865..1915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1714..1745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1872..1887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2372 AA; 266675 MW; 99FFA38863F75746 CRC64;
MTLLSSFFSR SLLFSLFTTS SLVSGLKYDA SLVEWNLNTN RSAQSPVDYA GDRGPDHKYF
PSPDNWRVPF YTLFLDRFVN GDPDNDDKNG TIYETDMFST QLRFGGDLDG LKDSLDYIAG
MGIKGIYIAG SPFINLPWGA DSYSPVDLTV LDKHFGTIKK WQEVVDEIHS RGMWVVLDNT
MATMSDLIGF VGYLNESTPF REEEHKVIWK NPDRRYLDFD IGNEYNETCD YPVFWYEDGR
RIKPPKLKGC YDSDFDQYGD IEAFGVWPDW KRQLAKFASV QDRLREWKPD VMARLIRFSC
MTIGTLDIDG FRIDKAVQVT VDAQAKFSSA MRECAKRYNK HNFIIYGEIT AGNTLGSIYL
GRGRDFDMTL KLQGDSVKAA SLRPDESDYF LREPGNTALD AGAFHYSIYR FMTRFLGLSG
NLEAGYDLPT DWVQAWEHMM LTNDFFNAYN NTRYDPRHLY GVTNQDVFRW PAIEMGEQRM
LLGYFIISLL LPGAPLVYYG EEQALYVLDG TASNYVYGRQ AFAPSPAWKN HGCFNLTIDQ
YIGWPVEKGR QGCNDPKVAY DHRDPSAHLR NTFRHMFRLR EELPVLKEGW LVKKLANQTY
PKLLNGSTKA TEFGIWSVVR DRHPSLQPDM AAQPVWLVYH NQGKRVEYEF DCNGKNPFIA
PFNAGTQVKN LFSDDDPITL GASNVQNEFT TGGKTAGCIS KITMEPYEFR AYVEPGRWVK
PHPMITKFTP GHDEPLNSTE YKGRVPFSIE YNTAMDCDSV TEALSAYVTV DGVNNATKLE
FESPKCESGI NNDNDYWVGY TGAIKSTWRI SSTLTNVPDG IIKITVGPSA TSRDGIRTNT
TDHFLLRLGK PDNPVVWPDS GSYSRDLLVI KNGQWYLNHA AAGATHWRYS TNWGSSWSDW
QPYPGSGLMS QPIKEQPWKG TKLQEWEGKH VMVQYYSKPL GSSAFIQHCD SNDVQFERGF
PHIRIHGPYN KWGYDAGLPG SMDLVHHHTW ELHYMYEWPA DFQLNIWGIN PDNQPDVGWI
YGDIDRDGIV DRLPPSSLAR NVINITAPPP MPALAYKLRY NDKTWRFEYI PSGHIGPQIL
IFILCAVMPV ATALAACWIY LGSFYQVKIN KSGFGRKGWI PLGLSNLSRL DLKSFGKGGV
EMSAITPSPS DNSKAVAPLP NKNGQRRTVL IATMEYNIDD FKIKIKIGGL GVMAQLMGSA
LTHMDLIWVV PTVGDVSYPF DKMEKAESMF VQVMGQPYEI EVYYYQSKNI TYVILDAPVF
RKQTKADPYI ARMDDIESAI LYAAWNSCIA ETIRRFPVDI YHINDYHGAA APLYLLPQTI
PCCLSLHNAE FQGMWPMRTP EEQKEVCDVF GLPMDVVKTY VQYGSVFNLL HAGASYLRIH
QRGFGAVGVS RKYGDRSLAR YPIFWSLKNI GHLPNPDPSD TAEWNPNMDI SKQSKDITID
QAFEEKRADL RRQAQEWAGL EVDPSAELFV FVGRWSMQKG IDLIADIFPS ILEKYPKTQL
ICVGPVIDLY GRFAALKLQK LMEMYPKRVY SRPEFTQLPP YIFSGAEFAL IPSRDEPFGL
VAVEFGRKGA LGVGARVGGL GQMPGFWYTV ESMTPSHLLQ QFKQAIVSAL ECKPQKRALM
RAWSAKQRFP VAQWVRQLDQ LYDESIRIHH KEAAKKKKVP HLAPSPNPSR PASPSSSATY
VDQTGAYDNI GIASPAPATL TPNRGLMTPD LPTPSAPWLS SRPGSPRASV ASNGGNGLYA
NPSARESTAS VDSFAIRAQR DGMPSPGLAP DVGGLAPPPP TLGQSHRNSS LLSLPDVVGD
RHDLKLQQVD QFFNDSNGEY QAQFEELLEG LTASNSASDL CIEAFLKKSE KEWFARYRDA
KLGRHRESRI NSPVSSRPAS RSGQRRNESV VSRGRQRHRS ITPSSMARSV FEHSPPPGQP
VDDEFLLGEG YQAPSGLKKW MSIRIGDWPI YSFLLALTQI ISISSYQIVL LTGETMQTPE
KLYTVAGVYI ASSLIWFAME RNFKSVYALS APWFFFGLAF LFIGIAPFIP DWRVANGIEQ
AATCFYAVGA SSGALAFALN FGDEGGSPTK QWITRALVVS GFAQVYSIGL WYWGSIVADT
DPTATVFVGK SNVPRAVVVG IPLAIVCWAI GTVLFVGLPD YYRQSPATIP GFWISLYRRK
IVPWFFVMII LQNYWLSAPY GRSWQFLFTT QHVPGWGIFL LALAFYVVLW AIVLYGFSYF
SDEHTWLLPI FAIGLCAPRW AQEFWGTSGI GWYLPWAGSA VGSTILSRCL WLWLGLLDNI
QGVGIGMMLL ATLTRHHVLA VLIGAQVIGS VFTMLARATS PNALSPHTTF PDFSQGAMPG
VAAPYFWVCL AFQLVIPVGF FKFFRKEQVM KP
//
