ID A7TP15_VANPO Unreviewed; 1899 AA.
AC A7TP15;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, 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 ORFNames=Kpol_499p12 {ECO:0000313|EMBL:EDO15984.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO15984.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480437; EDO15984.1; -; Genomic_DNA.
DR RefSeq; XP_001643842.1; XM_001643792.1.
DR STRING; 436907.A7TP15; -.
DR GeneID; 5544121; -.
DR KEGG; vpo:Kpol_499p12; -.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000844_0_1_1; -.
DR InParanoid; A7TP15; -.
DR OMA; AWTDFFI; -.
DR OrthoDB; 354539at2759; -.
DR PhylomeDB; A7TP15; -.
DR Proteomes; UP000000267; 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 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:UP000000267};
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 510..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 584..609
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 695..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 721..739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1378..1399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1465..1486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1492..1509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1580..1602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1622..1643
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1663..1686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1762..1782
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1823..1843
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 319..431
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 264..299
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 62..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1899 AA; 217732 MW; F86866892514BAE9 CRC64;
MSYNNNNMDN MGNPDGHPQD MNGMGYPQND QDYQGQAYDD YGQPIYPDQM HPQDEYYDPN
AMNDPYSQNP NGQGYYQQPY ENQNAGQGYP GDQYYDQPQM HQDPENFSDF SSYGPPATPG
YDNYGNMGQY TPSQVSYGDP NSSGTSTPIY GGMNYDPNAI AMTLPNDPYP AWTADNQSPV
SIEQIEDVFI DLTNRFGFQR DSMRNMFDHF MTLLDSRSSR MSPDQALLSL HSDYIGGDTA
NYKKWYFAAQ LDLDDEVGFR NMNLSKVKKK RRLMRKKNKK ALEETAEDTE ATLNQLEGDT
SLEAADYRWK AKMNQLSPLE RVRHIALYLL CWGEANQVRF TSECLCFIYK CALDYLDSPL
CQQRTEPMPE GDYLNRIITP LYRFLRNQVY EIVDNRYVKR EKDHNKIIGY DDVNQLFWYP
EGISKIVLED STKLIEIPIE ERYLRLGDVT WDDVFFKTFK ETRSWLHMVT NFNRIWIIHA
TVYWMYTAYN APSFYTKNYQ QLVDNQPLAA YRWASAALGG TLACALQIAA TVCEWLFVPR
NWAGAQHLSR RFWFLCGCLG VNLGPLIFVF AYDKDYVYST AAHAVAAVTF FIAVGTLIFF
SIMPLGGLFT SYMNKTSRRY VASQTFTANF APLHGIDMWL SYLVWVTVFA AKFSESYFFL
TLSLRDPIRI LSTTTMRCTG EFWWGDVMCK QQPKIVLGLM IATDFLLFFL DTYLWYVLVN
VIFSVGKSFY MGISILTPWR NIFTRLPKRI YSKILATTDM EIKYKPKVLI SQVWNAIVIS
MYREHLLAID HVQKLLYHQV PSEIEGKRTL RAPTFFVSQD DNNFETEFFP RNSEAERRIS
FFAQSLATPI PEPLPVDNMP TFTVLTPHYA ERILLSLREI IREDDQFSRV TLLEYLKQLH
PVEWECFVKD TKILAEETAA YDGNDEDPEK ANALKSQIDD LPFYCIGFKS AAPEYTLRTR
IWASLRSQTL YRTVSGFMNY SRAIKLLYRV ENPEIVQMFG GNAEGLEREL EKMARRKFKF
LVSMQRLAKF KPHELENAEF LLRAYPDLQI AYLDEEPPLQ EGDEPRIYSA LIDGHCEILE
NGRRRPKFRV QLSGNPILGD GKSDNQNHAL IFYRGEYIQL IDANQDNYLE ECLKIRSVLA
EFEELSVEQI NPYAPGLKYE EQNNNHPVAI VGAREYIFSE NSGVLGDIAA GKEQTFGTLF
ARTLSQIGGK LHYGHPDFVN GLFMTTRGGV SKAQKGLHLN EDIYAGMNAM LRGGRIKHCE
YYQCGKGRDL GFGTILNFTT KIGAGMGEQM LSREYYYLGT QLPIDRFLSF YYAHPGFHLN
NLFIQLSLQL FMLTLVNLNA LAHESILCFY NRNTPITDVL YPWGCYNFAP AIDWVRRYTL
SIFIVFWIAF IPIVIQELIE RGVWKATVRF FRHILSLSPM FEVFAGQIYS AALLSDLTVG
GARYISTGRG FATARIPFSI LYSRFAGSAI YMGARSLFML LFSTIAHWQA PLLWFWASLS
SLMFSPFVFN PHQFSWEDFF LDYRDFIRWL TRGNNKYHRN SWIGYVRMSR SRVTGFKRKL
IGDESEKAVG DASRAHRTNV IMAEIFPCAV YAAGCFVAFT FINAQTGVNQ TDNTDPTVNS
CLRIIICTLA PIAINLGVLF FCLGMSCCSG PLFGMCCKKT GSVMAGIAHG VAVIIHLAFF
IVMWVFEGFN FTRGLLGTIT CIQCQRLVFQ CMTVLMLTRE FKNDHSNTAF WTGKWYGSGM
GISAWTQPSR ELTAKVIEMS EFAADFILGH ILLFCQLPIL CIPRIDSFHS MMLFWLKPSR
QIRPPIYSLK QTRLRKRMVK KYISLYFCVL AGFAACIIGP AVASSHVSDK LGSGLTGVAH
NLFQPRNQSN NDTGPSFSTF SRASDYTSAP KLKTWSTIK
//
