ID O13428_CANAX Unreviewed; 1897 AA. AC O13428; DT 01-JAN-1998, integrated into UniProtKB/TrEMBL. DT 01-JAN-1998, sequence version 1. DT 03-MAY-2023, entry version 57. 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 Name=GSC1 {ECO:0000313|EMBL:BAA21535.1}; OS Candida albicans (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=5476 {ECO:0000313|EMBL:BAA21535.1}; RN [1] {ECO:0000313|EMBL:BAA21535.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=9209021; RA Mio T., Adachi-Shimizu M., Tachibana Y., Tabuchi H., Inoue S.B., Yabe T., RA Yamada-Okabe T., Arisawa M., Watanabe T., Yamada-Okabe H.; RT "Cloning of the Candida albicans homolog of Saccharomyces cerevisiae RT GSC1/FKS1 and its involvement in beta-1,3-glucan synthesis."; RL J. Bacteriol. 179:4096-4105(1997). 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}. 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; D88815; BAA21535.1; -; Genomic_DNA. DR BindingDB; O13428; -. DR ChEMBL; CHEMBL2364673; -. DR ChEMBL; CHEMBL4844; -. DR DrugCentral; O13428; -. DR CAZy; GT48; Glycosyltransferase Family 48. DR VEuPathDB; FungiDB:C1_02420C_A; -. DR VEuPathDB; FungiDB:CAWG_01443; -. 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 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 495..519 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 534..552 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 564..585 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 624..646 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 677..700 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1362..1383 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1449..1469 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1475..1493 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1565..1586 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1612..1639 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1651..1675 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1681..1707 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1719..1736 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1756..1775 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1813..1833 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 301..413 FT /note="1,3-beta-glucan synthase component FKS1-like" FT /evidence="ECO:0000259|SMART:SM01205" FT REGION 1..44 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 113..139 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1897 AA; 217983 MW; 00CDF2C9A19B89FC CRC64; MSYNDNNNHY YDPNQQGGMP PHQGGEGYYQ QQYDDMGQQP HQQDYYDPNA QYQQQPYDMD GYQDQANYGG QPMNAQGYNA DPEAFSDFSY GGQTPGTPGY DQYGTQYTPS QMSYGGDPRS SGASTPIYGG QGQGYDPTQF NMSSNLPYPA WSADPQAPIK IEHIEDIFID LTNKFGFQRD SMRNMFDYFM TLLDSRSSRM SPAQALLSLH ADYIGGDNAN YRKWYFSSQQ DLDDSLGFAN MTLGKIGRKA RKASKKSKKA RKAAEEHGQD VDALANELEG DYSLEAAEIR WKAKMNSLTP EERVRDLALY LLIWGEANQV RFTPECLCYI YKSATDYLNS PLCQQRQEPV PEGDYLNRVI TPLYRFIRSQ VYEIYDGRFV KREKDHNKVI GYDDVNQLFW YPEGISRIIF EDGTRLVDIP QEERFLKLGE VEWKNVFFKT YKEIRTWLHF VTNFNRIWII HGTIYWMYTA YNSPTLYTKH YVQTINQQPL ASSRWAACAI GGVLASFIQI LATLFEWIFV PREWAGAQHL SRRMLFLVLI FLLNLVPPVY TFQITKLVIY SKSAYAVSIV GFFIAVATLV FFAVMPLGGL FTSYMNKRSR RYIASQTFTA NYIKLKGLDM WMSYLLWFLV FLAKLVESYF FSTLSLRDPI RNLSTMTMRC VGEVWYKDIV CRNQAKIVLG LMYLVDLLLF FLDTYMWYII CNCIFSIGRS FYLGISILTP WRNIFTRLPK RIYSKILATT EMEIKYKPKV LISQIWNAIV ISMYREHLLA IDHVQKLLYH QVPSEIEGKR TLRAPTFFVS QDDNNFETEF FPRNSEAERR ISFFAQSLAT PMPEPLPVDN MPTFTVFTPH YSEKILLSLR EIIREDDQFS RVTLLEYLKQ LHPVEWDCFV KDTKILAEET AAYENGDDSE KLSEDGLKSK IDDLPFYCIG FKSAAPEYTL RTRIWASLRS QTLYRTVSGF MNYARAIKLL YRVENPELVQ YFGGDPEGLE LALERMARRK FRFLVSMQRL SKFKDDEMEN AEFLLRAYPD LQIAYLDEEP ALNEDEEPRV YSALIDGHCE MLENGRRRPK FRVQLSGNPI LGDGKSDNQN HAVIFHRGEY IQLIDANQDN YLEECLKIRS VLAEFEEMNV EHVNPYAPNL KSEDNNTKKD PVAFLGAREY IFSENSGVLG DVAAGKEQTF GTLFARTLAQ IGGKLHYGHP DFLNATFMLT RGGVSKAQKG LHLNEDIYAG MNAMMRGGKI KHCEYYQCGK GRDLGFGSIL NFTTKIGAGM GEQMLSREYF YLGTQLPLDR FLSFYYGHPG FHINNLFIQL SLQVFILVLG NLNSLAHEAI MCSYNKDVPV TDVLYPFGCY NIAPAVDWIR RYTLSIFIVF FISFIPLVVQ ELIERGVWKA FQRFVRHFIS MSPFFEVFVA QIYSSSVFTD LTVGGARYIS TGRGFATSRI PFSILYSRFA DSSIYMGARL MLILLFGTVS HWQAPLLWFW ASLSALMFSP FIFNPHQFAW EDFFLDYRDF IRWLSRGNTK WHRNSWIGYV RLSRSRITGF KRKLTGDVSE KAAGDASRAH RSNVLFADFL PTLIYTAGLY VAYTFINAQT GVTSYPYEIN GSTDPQPVNS TLRLIICALA PVVIDMGCLG VCLAMACCAG PMLGLCCKKT GAVIAGVAHG VAVIVHIIFF IVMWVTEGFN FARLMLGIAT MIYVQRLLFK FLTLCFLTRE FKNDKANTAF WTGKWYNTGM GWMAFTQPSR EFVAKIIEMS EFAGDFVLAH IILFCQLPLL FIPLVDRWHS MMLFWLKPSR LIRPPIYSLK QARLRKRMVR KYCVLYFAVL ILFIVIIVAP AVASGQIAVD QFANIGGSGS IADGLFQPRN VSNNDTGNHR PKTYTWSYLS TRFTGSTTPY STNPFRV //