ID A0A2J6TWC4_9HELO Unreviewed; 2479 AA.
AC A0A2J6TWC4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JUN-2023, entry version 21.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
DE AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase {ECO:0000256|ARBA:ARBA00031935};
GN ORFNames=K444DRAFT_515472 {ECO:0000313|EMBL:PMD67329.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD67329.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD67329.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD67329.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC Evidence={ECO:0000256|ARBA:ARBA00000192};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000256|ARBA:ARBA00009040}.
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DR EMBL; KZ613740; PMD67329.1; -; Genomic_DNA.
DR STRING; 1095630.A0A2J6TWC4; -.
DR InParanoid; A0A2J6TWC4; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000235371; Unassembled WGS sequence.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR12741:SF29; 1,3-BETA-GLUCAN SYNTHASE COMPONENT FKS1-RELATED; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000235371};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PMD67329.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 498..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 542..565
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..603
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 674..696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 728..751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1351..1370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1403..1424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1606..1631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1654..1681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1693..1716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1722..1742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1850..1874
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 352..464
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2479 AA; 281606 MW; 7EEF77BE1AE45837 CRC64;
MSGHPQQQGH YDDGYGHHQQ GNTDSYYQDD GQGYYDQHGG YPEQGHHQGG DGYYDESGYY
NADANNPYHQ DGGYYEGQEH GGQYQDEYYN DQYYDQGAPA AGQHPQGQGY PKRRGDSEED
SETFSDFTMR SDMARATDMD YYGRGDERYT YNESQMGGRG YRPPSSQISY GGNRSSGAST
PNYGMEYNNN VLPAGQRSRE PYPAWTSDAQ IPLSKEEVED IFLDLTAKFG FQRDSMRNMY
DHLMTLLDSR ASRMTPNQAL LSLHADYIGG DNANYRKWYF AAHLDLDDAV GFANMKLGKA
NRRTRKARRA AKKKQQLDPQ NEQQTLEQLE GDNSLEAAEY RWKTRMNRMS QHDRVRQLAL
YLLCWGEANQ VRFMPECLCF IFKCADDYLN SPACQNLVEP VDEFTYLNNV ITPLYQYCRD
QGYEIQDGKY VRRERDHNKV IGYDDCNQLF WYPEGIELIV MEDKTRIVDF PPAERFLKLK
DVNWKKVFFK TYKETRSWFH MLVNFNRIWV IHITSFWFYT AKNSPTLLVK NYEQQLNNLP
PASAQWSAVA LGGAIACLIQ IAATIAEWTY VPRRWAGAQH LTRKLLFLIL MFVINVGPSV
YIFGFKDVQA TKIAFILGIV QFFIALATFF FFAIMPLGGL FGSYLTKNSR QYVASQTFTA
SYPRLTGNDM WMSYGLWLCV FVAKLAESYV FLTLSFRDPI RYLASMEITS CQGDALIKFA
LCKYQPKILL VLMFITDLCL FFLDTFLWYI IMNTIYSVAR SFYLGVSIWT PWRNIFSRLP
KRIYSKVLAT TDMEIKYKPK VLISQIWNAI VISMYREHLL AIDHVQKLLY HQVPSEQEGK
RTLRAPTFFV SQEDHSFKTE FFPSQSEAER RISFFAQSLS TPIPEPLPVD NMPTFTVLIP
HYSEKILLSL REIIREDEPY SRVTLLEYLK QLHPHEWDCF VKDTKILADE TSQFNGDYEK
SEKDTAKSKI DDLPFYCIGF KSAAPEYTLR TRIWASLRSQ TLYRTISGFM NYSRAIKLLY
RVENPEVVQM FGGNSDKLER ELERMARRKF KLVVSMQRYA KFHKEEMENT EFLLRAYPDL
QIAYLDEEAP LVEGEEPRLY SALIDGHSEI MENGMRRPKF RIQLSGNPIL GDGKSDNQNH
AIIFYRGEYI QLIDANQDNY LEECLKIRSV LAEFEEMVTD NVSPYTPGVE TLKTNPVAIL
GAREYIFSEN IGILGDVAAG KEQTFGTLFA RTLASIGGKL HYGHPDFLNG IFMTTRGGVS
KAQKGLHLNE DIYAGMTALL RGGRIKHCEY YQCGKGRDLG FGSILNFTTK IGTGMGEQML
SREYYYLGTQ LPLDRFLSFY YAHPGFHLNN MFIMLSVQMF MICLINLGAL RNQTIACTYN
KNVPITDPLF PTGCANTQPV LDWVYRCTIS IFIVFFISFV PLVVQELTER GVWRAATRLG
KQFCSLSPFF EVFVCQIYAN SVQQDLSFGG ARYIGTGRGF ATARIPFGVL YSRFAGPSIY
LGARSLMMLL FATLTVWQPA LVYFWVTLLA MCMSPFIYNP HQFAWNDFFI DYRDFLRWLS
RGNSRSHQSS WIGFCRLSRT RITGYKRKAL GDPSSKMSGD VPRASFANLF FGEIVGPLLI
VVVTLLPYLF INSQVGVTSV TNPDATDLHA TNSLIRVGIV ALAPIAINAG VLAAMFGMAC
CMGPILSMCC KKFGSVLAAI AHGVSVVMLL VLWEAMFFLE GFVFAKALLG MIAATAIQRF
VYKLIIALAL TREFKSDTSN IAFWTGKWYS MGWHSMSQPA REFLCKITEL GMFAGDFVLG
HVLLFVMLPV IAIPHVDKAH SVLLFWLRPS RQIRPPIYSM KQSKLRKRRV WRYAVLYFVM
LVVFLALIVG PIVASPIITS STKSLSVPMQ LLQPVGLKNN DTLNDTQTGT GAPGRAATIS
SAISIPNPRC RPSQNFWKPQ LKHDSPQRPI AMSIFNSSLE NMEFQDAQRF VIRSVHEITA
RFQKVPGSAM LIRYIQSSYQ DDPVRSAIEL VLVIFFVRYL LSPSYSTKDG NFVKLTEEEI
DDLVDEWTPE PLVAPQTAFE EAENEKTPVV VGPTGPKVKL SNGRTVTNLA SYNFYNFVGN
EQVKEKAIQT LRTYGVGPCG PPQFYGTQDV HMKTEADIAS CLGTEKCIVY AQAFSTISSV
IPAFCKRGDI IVADRAVNYA IRKGLQICRS TIRYYEHNNM EDLERVLQKV VKEQAKKPLT
RRFIVTEGLF ETVGDCVDLP KLVELKLRYK FRLMLDETWS FGVLGRTGRG LTEAQNVDAS
QVDMIVGSLA GPLCAGGGFC AGTTDVVAHQ RITAAAYTYS AALPAMLATT ASETLNMLQT
NPEILVQCRE NIKTMRQQLD PRSDWVHCTS SPENPIILLV LKPDVINSRR LSVEEQERVL
QECVDETLLN GVLITRLKSM PLSPGGKDED WKLQPALKVC ITTGLSKKEI EKAGVTIRHA
ITKVLTRKSS SKLALPAVA
//
