ID S7QFE5_GLOTA Unreviewed; 1646 AA.
AC S7QFE5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 03-MAY-2023, entry version 33.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
GN ORFNames=GLOTRDRAFT_35804 {ECO:0000313|EMBL:EPQ58132.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ58132.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ58132.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ58132.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; KB469298; EPQ58132.1; -; Genomic_DNA.
DR RefSeq; XP_007862859.1; XM_007864668.1.
DR STRING; 670483.S7QFE5; -.
DR GeneID; 19305658; -.
DR KEGG; gtr:GLOTRDRAFT_35804; -.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000844_0_1_1; -.
DR OMA; IFVVAYM; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000030669; 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:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
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; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 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:UP000030669};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 272..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 493..510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1118..1137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1168..1189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1273..1303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1374..1396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1416..1440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1452..1475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1482..1506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1555..1574
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1608..1632
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..235
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1646 AA; 188190 MW; 328CAA2549587D37 CRC64;
MSTEEIEDIF LDLTQKFGFQ RDSMRNMFDF LMQQLDSRAS RMTPNQALLT LHADYIGGQN
ANYRKWYFAA QLNLDDAVGQ SQNPGLQRLK SIGGKGAPKT AGTKSLDSAL NRWRNAMNNM
SQYDRLRQVA LYLLCWGEAG NVRFVPECLC FIFKCADDYY RSSECQNRVE PVREGLYLET
IIKPLYRFMR DQGYEVVDGK FVRKEKDHDQ IIGYDDINQL FWYPEGIARI VLDNNSRLVD
LPAPQRFMKL GRVDWNRVFF KTYFEKRSTA HLLVNFNRIW ILHIAVFWFY TAYNSPRVYA
PHDKQFPSAP MTWSATALGG AVATLIMIFA TLAEYTYIPT TWNNASHLTT RLFFLCIVLA
LTGGPTIYIA KVDGLPTPNQ IPLILGVVQF GISVVATIAF GIIPSGRMFG DRVAGKSRKY
MASQTFTASY PELPRGARTA SILLWVLVFG CKFTESYFFL TESFSSPIAV MARTKVQGCN
DKYFGNALCT NQVPFTLAIM YVMDVILFFL DTYMWYIMWN VVFSIFRSFS LGLSIWTPWQ
EVYTRMPKRI YAKLLATGEM EVKYKPKVLV SQVWNAIIIS MYREHLLSID HVQRLLYHQV
DGPDGKRTLR APPFFTNNDG NSGKFLPAGG EAERRISFFA SSLTTALPDP LPVDAMPTFT
VLVPHYSEKI LLSLREIIRE EDQNTRVTLL EYLKQLHPVE WDNFVKDTKI LAEESSFSDT
TSSPFGTQNE KRGSKADDLP FYCIGFKTAA PEYTLRTRIW ASLRAQTLYR TVSGMMNYAK
AIKLLYRVEN PQIVQMFAGN TERLERELER MSRRKFKFAI SMQRYSKFNK EEMENAEFLL
RAYPDLQIAY LDEEVGPKGS EPKIYSALID GHSEIDEKTG KRKPKFRVEL PGNPILGDGK
SDNQNHAIIF YRGEYLQLID ANQDNYLEEC IKIRNILGEF EEYSISQQSP YAQWGHKEFK
KSPVAIIGTR EYIFSENIGV LGDIAAGKEQ TFGTMTARAL AWIGGKLHYG HPDFLNAIFM
NTRGGVSKAQ KGLHLNEDIF AGMNAFGRGG RIKHSEYYQC GKGRDLGFGT ILNFQTKIGT
GMGEQLLSRE YYYLGTQLPL DRFLTFYYGH PGFHINNILV IYSIQVFMVT LLFIGTLNKQ
LSICQVDSDG NVLGGQPGCY NLIPVFDWIK RCIVSIFLVF FIAFLPLFLQ ELVERGTGSA
LIRLGKHFLS LSPFFEVFST QIYSQAVLSN LTYGGARYIA TGRGFATTRI SFATLYSRFA
GPSIYMGMRN LLLLLYSSLA LWIPHLIYFW FSVLSLCIAP FLFNPHQFSF ADFVIDYREF
LRWMCRGNSR TKASSWYGYC RLSRTMITGY KKKKLGHPSE KLSGDVPRAS WRSVIFAEVI
WPICVATIFV IAYMFVKSFP DRNGNPNPSP LIRIGVVSIG PVVWNAAVLL SLFFISLFMG
PMLEGWAKFA SVMAATAHLL CLIGYVAFFE FFWFLELWDV SHAVLGVICI IAIQRAIQKI
LIAVFLSREF KHDETNRAWW TGKWYGRGLG SSAMSQPARE FIVKIVEMSL WSSDFLLGHI
LLVILTPPVL IPYFDRLHST MLFWLRPSKQ IRPPLFSTKQ KRQRRWIIIK YSFAYIIAVG
AIAALIVLPS LFRDDITFNC TVCSNI
//
