ID A0AAI9SYK3_9ASCO Unreviewed; 2186 AA.
AC A0AAI9SYK3;
DT 24-JUL-2024, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2024, sequence version 1.
DT 28-JAN-2026, entry version 6.
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=KGF56_001814 {ECO:0000313|EMBL:KAI3405367.2};
OS Candida oxycetoniae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=497107 {ECO:0000313|EMBL:KAI3405367.2, ECO:0000313|Proteomes:UP001202479};
RN [1] {ECO:0000313|EMBL:KAI3405367.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 10844 {ECO:0000313|EMBL:KAI3405367.2};
RX PubMed=35438177; DOI=10.1093/dnares/dsac010;
RA Mixao V., Del Olmo V., Hegedusova E., Saus E., Pryszcz L., Cillingova A.,
RA Nosek J., Gabaldon T.;
RT "Genome analysis of five recently described species of the CUG-Ser clade
RT uncovers Candida theae as a new hybrid lineage with pathogenic potential in
RT the Candida parapsilosis species complex.";
RL DNA Res. 29:dsac010-dsac010(2022).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + UDP + H(+); 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:ARBA00047777};
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAI3405367.2}.
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DR EMBL; JAHUZD010000038; KAI3405367.2; -; Genomic_DNA.
DR RefSeq; XP_049181112.1; XM_049322977.1.
DR GeneID; 73379431; -.
DR Proteomes; UP001202479; Unassembled WGS sequence.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
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 GO; GO:0051278; P:fungal-type cell wall polysaccharide biosynthetic process; IEA:TreeGrafter.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR056261; FKS1-like_dom2.
DR InterPro; IPR003440; Glyco_trans_48_dom.
DR PANTHER; PTHR12741:SF48; 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; PF23605; FKS1_dom2; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP001202479};
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 290..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1124..1145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1157..1180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1218..1235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1241..1259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1322..1343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1363..1388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1400..1423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1429..1455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1502..1523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 152..256
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 109..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1637..1686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2059..2136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1715..1749
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 116..127
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1591..1600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1618
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1661
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1675..1686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2059..2069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2113..2126
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2186 AA; 251795 MW; 9286D070806161CB CRC64;
MGFKDNQYHA WCEENEGNIT PERILAIFNN LATKYGFQDD NVRNIYALFM TQLDSRSSRM
SGSCALKSLH MNYIGGLNSN YKNWYLSAQY FYEDDENWTP KKKKKKKRMK KSTKIDDDDD
GDGDDDGGGG GGFDGEDEED RWLRKFRNCT EEDYVYQVAL YLLIWGEANN IRFMPECLCF
IYQCALDYQG ENFEKFYFLD KIITPLYSFL RDQQYKLIGD RWKRKEVDHS QTIGYDDVNQ
HFWSRQGLNK LKLYSGEVFY EIKKESRFKE ICQINWQKSL SKTYRERRTW IHVLTNFNRI
WIIHVSMFWY FMSFNSPSLY TRDYTPEKTP LLHIRLAIVS AGGTIAALIS LFATISEFLF
IKSKNFKKLA ILLLLLVLNT APITYNLVIL KWNEYSHLGN IFAGLMLTVS IITFVYLSIV
PFGSIDSIFA TSFPKLRLRN RLFSVFLWVT VFAAKNSESY FFLILSLKDP IQILSSIELE
CNSGHFLCKF QPKITLFLFY LTDLILFFLD TYLWLPDRVL TKIYYGESMN LILVISQIWN
SIIISMYREH LLSVEQVGKL IYQKEFEDEN IRPPLFFVNE DDNTFKLHAF IKTEEEWERR
ITFFAQSLSS PLPEPFPVVS IPSFTVLIPH YSEKILLSLK DLIKEQSFSK LSLLEYLKQL
HSNEWESFVQ DSKMISNLDK LEGEGEGEGE EETKFEKFED LPYYCIGFKD SSAENVLRTR
IWAALRCQTL YRTVSGFMNY ETALKILYRS ENIGLDAEND LFIEEELQEF VDRKFCLLVA
MQKYQNFSND ASADAEALFR AFPNICVAIL ETEGNAYYST LLDVSHRDSR GEYIKKYRIK
LSGNPILGDG KSDNQNNALI FYRGEYIQVI DANQDNYIEE CLKIKSLLTE FEEIDIKVTN
AYEPYKVAPI HEKKQQQYPP VAIVGAREFI FSQNVGILGD IAAGKEQTFG TLFARTMGEI
GSKLHYGHPD FLNGIFMTTR GGISKAQRGL HLNEDIYAGI TATCRGGRIK HCDYYQCGKG
RDLGFQSIVN FTKKIGAGMG EQLLSREYFY LGTKLPIDRF LSFYYAHPGF HINNLSIMLS
VKIFMLLVAN LGSLNYINIP CERKEGGGNN DIPGCHNLVP VLNWIDRFVL SVFVCFFISF
LPLIIQELIE KGFIRSIFRI VLHITSLSPF FEVFICQVYS RALRDNFVFG EAQYIATGRG
FAISRVSFSL LYTRYANLSI YCGGEILLVV LFGMMTVGRN ALLWFVITIV SLCLAPFLFN
PHQFNFIDFF VDYREFIRWL SRGNTKPKES SWISFTKNVR SRLTGEKSQG CLSGRSSTTI
NLLLGEVVAP SIGLVSYVIP FLYLHSNHSL IELSLSNPLI KLALAMVVPY VANIAILATI
WATSVTLAPI FALCIKRTPA FFAGVAHFLS ILINIINIEV FFFLEEWNFV HLISALLVLF
SFHRVISNFI LIVAVSRERQ ENVTNEAWWS GKWYKSGLGI AVVSQNVREL IIKILELNKF
SFDFLLGHIC LFTMFPIVLI PYIDTLHTID GIGRWYRSTT IDMKPLTKAD LLRQFADDQE
DEIFGDIENV DFGPGTGTAA TRNKVGKSTR RQYEKEKEAK NGGGSGMGAG TSTGMGTGGD
DDDAIETLKV NQLNLNTHNS PSFQLTPKNG GSSSPTKSTK SSGKRITRDA LSEYSEGNEN
NDTDITSEFS QDEFEGWDEC FNKNNQNQSI YQQMNQRLIA RKVAQQREAE REQQELIQMR
QQQQQHQQNK NTRVLLFKES PKSERFKDGG HKLTNENLSL LDQLETERTI NYEYTRDDYD
EFEEGFNEAE LEESISKIQP LRRIQLQQLH MQQPSSSYGT RKLSNKQSMP SLARNNVSIM
KKFKSSMDLH GRINEENEED IYEQPQFNYN NRVIKRLDRI PSYYSKPALI NTEDRNQILD
KFKETKSKHI HGRNRKMGNL RHLKPTTITT TAATDIPIQH QKSAMRFNKQ KSVWEGNEVD
LLRFEKKPSL ITSKDIQPRS SAIGTGLSCK KQGNMLYDEK NLRWINLEEG GGGEDEMIFD
DIPDLTDPVE TLTQYNVPQQ LSQLSQRGSP SKKKNNNNDD ICIVQSSSSS PPPPPPLPLS
SRRGLCSQYT QRTVSTATSH TASSSTQSDH NYKHERKELK LSDKLVDKFL KEEQKIERKI
GHWFIGTNEA KRDYYWEIRK MVTEED
//
