ID Q6C549_YARLI Unreviewed; 1934 AA.
AC Q6C549;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 2.
DT 27-MAR-2024, entry version 86.
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=YALI0_E21021g {ECO:0000313|EMBL:CAG79808.2};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG79808.2, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG79808.2, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382131; CAG79808.2; -; Genomic_DNA.
DR RefSeq; XP_504213.2; XM_504213.2.
DR STRING; 284591.Q6C549; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR EnsemblFungi; CAG79808; CAG79808; YALI0_E21021g.
DR GeneID; 2911849; -.
DR KEGG; yli:YALI0E21021g; -.
DR VEuPathDB; FungiDB:YALI0_E21021g; -.
DR HOGENOM; CLU_000844_0_1_1; -.
DR InParanoid; Q6C549; -.
DR OMA; AWTDFFI; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IBA:GO_Central.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0051278; P:fungal-type cell wall polysaccharide biosynthetic process; IBA:GO_Central.
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:UP000001300};
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 471..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 519..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 558..577
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 589..615
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 648..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 723..749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1334..1354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1388..1409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1499..1523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1595..1618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1630..1663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1675..1696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1702..1727
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1833..1853
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 325..437
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1934 AA; 221554 MW; 2663DB0F545DF944 CRC64;
MSYDYNYDYQ QPGQQGGDGQ HNGQNQQHPG QQEYYDDYYD DGYGNQYGAQ EGYQEGVDQH
GNPYQHDPHA GVAAATSGGY RNVKDDGSET FSDFTEQNGQ GYNQYNQGYN QGQYNQGYQG
QYNQGYGGYD QYGQYNDASQ ISFRSSGAST PIYGLDYAAS QQGIGAGSGH SREPYPAWSA
DNQVPVTKEE IEDVFIDLTN KFGFQRDSMR NMYDFLMVLL DSRSSRMTPN QALLSLHADY
IGGDNANYRK WYFAAQLDLD DDIGFRNMKL GKTNKRTRKA RKKFRKEMQD PDADPAKTLE
EIEGDNSLEA AEYRWKTKMN ALSPLERVRH IALWLLCWGE ANQVRFTPEC LCFIFKCADD
YYTSAECQQR VEPVEEGDYL NRIITPLYRF IRGQGYEIFD GKFVKRERDH NKVIGYDDVN
QLFWYPEGIE RITFEDESRL VDVPQSERYM KLGDVIWDKV FFKTYKETRS WFHVFVNFNR
IWIIHVTFYW YYASFNSPTL YMKNYVPTLD NHPPPACKWG AGAIGGVIAT GLQIIATLSE
WAFVPRKWAG AQHLTRRLMF LIGILIVNLV APVYVLGVVG TTHESTSALA VGIVGFIISI
FTFIFFSIMP LGGLFTSYMK KSTRRYVASQ TFTNSYPRLE FHDKIMSYLL WVCVFGAKLS
ESYYFLILSL RDPIRDLSQM KMRCFGEKWF GVEYHDALCK VQPQITLGLM YATDLILFFL
DTYLWYIICN TIFSVARSFY LGISIWTPWR NIFSRLPKRI YSKILATTDM EIKYKPKVLI
SQIWNAIVIS MYREHLLAIE HVQKLLYHQV PSEVEGKRTL RAPTFFITQD DHAFETEFFP
RNSEAERRIS FFAQSLSTPI PEPLPVDNMP TFSVLVPHYS EKILLSLREI IREDDQFSRV
TLLEYLKQLH PVEWDCFVKD TKILAEETAG FGEGSNDDLA EKDSDEVKAK IDDLPFYCIG
FKSAAPEYTL RTRIWASLRS QTLYRTVSGF MNYSRAIKLL YRVENPEVVQ MFGGNTEKLE
RELERMARRK FKFIVSMQRL TKFKPDEMEN TEFLLRAYPD LQIAYLDEEP PLNEGEEPRL
FSALIDGHCE ILENGRRRPK FRIQLSGNPI LGDGKSDNQN HALIFHRGEY IQLIDANQDN
YLEECLKIRS VLAEFEELNV ENVNMSPYTP GVNNKTPCPV AILGAREYIF SENIGILGDI
AAGKEQTFGT LFARTLAQIG GKLHYGHPDF LNSIFMCTRG GVSKAQKGLH LNEDIYAGMN
ALLRGGRIKH CEYYQCGKGR DLGFGSILNF TTKIGTGMGE QMLSREYYYL GTQLPLDRFL
SFFYAHPGFH INNLLIITSV QMFMIVMMSI GPLAHETKET ICWYDKDKPI TDPQTPVGCY
NLKPVLDWIR RCVLSIFIVF FISFVPLVVQ ELTERGVFRA AFRFARHFMS LSPLFEVFVC
QVYANSFIND LAFGGARYIA TGRGFATARL PFSVLYSRFA GDSIYLGARS TLMLLFGTIA
MWQAALLWFW VTLIAMCISP FVFNPHQFAW TDFFIDYRDF IRWLSRGNAK WHKNSWIGYV
RLTRTRITGY KRKVLGDESE KGAGDLSRAG ISNVFITEIF LPLIVAAFCF CGFTFINAQT
GVAEPVIVNS ILRIVICAIG PIVINAGLLL VLVCISCCAG PMLGLCCKKT GPVMAGIAHG
IAVIIHLIFF ELMWFFEGWS FVKGLCGTVT AIAIMRLIFN ILTILCLTRE FKHDHANQAW
WTGKWYGAGL GWASISQPFR EFVCKLIEMS LFAGDFYLGH WLLFFQLPVL CVPYIDKWHS
MMLFWLRPSR QIRPPIFSLK QNQLRKRIVK KYATLYFIIL IIFLVVLIAP AVAGPTMSMD
SLESLAGGKA DNDSIQDTNI LKGLIQVRSQ NQNDTGRCST GNGTECLLPT TGSWSTHVWW
TFTPSHTTSY STKP
//
