ID A0A164ZBX4_XYLHT Unreviewed; 2266 AA.
AC A0A164ZBX4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=L228DRAFT_254642 {ECO:0000313|EMBL:KZF18912.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF18912.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF18912.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF18912.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
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; KV407469; KZF18912.1; -; Genomic_DNA.
DR RefSeq; XP_018184467.1; XM_018333844.1.
DR STRING; 1328760.A0A164ZBX4; -.
DR GeneID; 28898981; -.
DR InParanoid; A0A164ZBX4; -.
DR OMA; AWTDFFI; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000076632; 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:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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; PF00155; Aminotran_1_2; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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:UP000076632};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZF18912.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 490..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 535..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 577..596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..622
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 694..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1244..1266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1287..1308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1379..1412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1480..1504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1524..1548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1560..1585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1591..1616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1628..1644
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1664..1683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1717..1741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 344..456
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2266 AA; 259058 MW; 1C98466B01D394B2 CRC64;
MSAQPHGQYD DAYGHHPEST GSYYQDDANE GYYDHQRDYQ QPQAGEGYYD DAGYYNAENT
NPYQEGGYYD AHPQGYQDEY YHDQYYDQNA AAGAQPGYGP KGKRRGPDSE EESETFSDFT
MRSDMARAAE LDYYGRGDEK YNSYGDGAMG ARGYRPPSSQ ISYGGNRSSG ASTPVYGMDH
PNVLPAGQRS REPYPAWTSD AQIPLSKEEI EDIFLDLTAK FGFQRDSMRN MYDHFMTLLD
SRASRMTPNQ ALLSLHADYI GGENANYRRW YFAAHLDLDD AVGFANMKLG KSSRRARKAR
KAAKKKAQQD PQNEEQTLES LEGDNSLEAA EYRWKSRMNR MSQHDRVRQV ALYLLCWGEA
NQVRFMPEAL CFIFKCADDY LHSPECQNRV DPVEEFTYLN EVITPLYQYC RDQCYEIQNG
KYVRRERDHE KVIGYDDINQ LFWYPEGIER IIFEDKTRLV DFPPGERFSK LKDVNWKKVF
FKTYKETRSW FHMLVNFNRI WVIHVCTYWF YTAYNSPSLY TKDYKQQIDN KPTHAAMWSA
PGFAGTIASL IEIAATICEW AYVPRKWAGA QHLTKRLLFL LLVFAVNLGP GIYVFGVNQH
GKIALILGVV QFFIAIATFF FFANSRHYPR LRGNDMWMSW GLWFLVFLCK LVESYFFLTL
SLRDPIRILG ETKIHRCAGD GIIKDKLCYH QPKILLGLMF FTDLVFFFLD TYLWYIIWNT
IFSVARSFYL GVSIWTPWRN IFSRLPKRIY SKILATTDME IKYKPKVLIS QIWNAIVISM
YREHLLAIDH VQKLLYHQVP SEQEGKRTLH HSFKTEFFPP LSEAERRISF FAQSLSTPIP
EPLPVDNMPT FTVFIPHYSE KILLSLREII REDEPFSRVT LLEYLKQLHP HEWDCFTSQF
NGDYEKTEKD TAKAKIDDLP FYCIGFKSAA PEYTLRTRIW ASLRSQTLYR TISGFMNYSR
AIKLLYRVEN PEVLERELER MARRKFKICV SMQRYAKFTT EERENTEFLL RAYPDLQIAY
LDEEPPVNEG EEPRLYSALI DGHSEILDNG MRRPKFRSDN QNHAIIFYRG EYIQLIDANQ
DNYLEECLKI RSVLAEFEEM TTDNVSPYTP GLPSTRFNPV AILGAREYIF SENIGILGDI
AAGKEQTFGT LFARTLAQIG GKLHYGHPDF LNGIFMTTRG DIYAGMNAVL RGGRIKHCEY
FQCGKGRDLG FGSQMLSREY YYLGTQLPLD RFLSFYYAHP GFHLNNLFIM LSVQFLMVCV
MNLGALRHET IMCHFKRGIP RTDPRTPTGR CIVSIFIVFF ISFVPLVVQE LTERGFWRAA
TRLAKQFSSL SPFFEIFVTQ IYANSLGQDL SFGGARYIGT GRGFATARIP FGVLYSPRAL
LMLLFGTVTV WVPWFLYFWV SLLALCISPF LFNPHQFSWN DFFIDYRDYL RWLSRGNSRS
HASSWIAFCR LSRTRITGYK RKILGDPSQK LSGDAPRAHF TNLFFAEIVG PLVWIGVSLI
PYLFINAQTG VKNPQPASNA LIRVAIVAMG PVAVNAGVLL GFFGMACCMG PLLSMCCKKF
GAVLAAIAHA IAVIVLLVFF EVMFFLEGWN FARTLLGMIT VITIQRFFFK LIICLALTRE
FKQDSANIAW WTGKWYAMGW HSISQPGREF LCKITELGFF AADFILGHFI LFLMLPALCV
PYIDKFHSVM LFWLRPSRQI RPPIYSLKQS KLRRRRVIRF AILYFVMVVI FVALIAAPLV
AGKVVHNLPS IPFDLRQPTH QNNNDTTNLR TGTALIPVGS SPTASSEASS GAAYQNDPVR
SAVELFLFLF AVRYLLSSKY STQKQNYVSL SDEEIDELVE DWSPEPLVPT QSTFEIAENE
KRPVIVGPTG PKTKLSNGRT VSNLASFNFY NFVANESLKE KAIQTLRTYG VGPCGPPGFY
GTQDVHMKTE ADIAAHLGTP ACIIYSQAFS TISSVIPAFS KRGDIIVADK SVNYAIRKGL
QISRSTVRWF EHNDMTDLER VLEKVVNEQA KKPLTRRFIV TEGLFENVGD VVNLPKLIEL
KLKYKFRLIL DETWSFGVLG RTGRGVTEQQ NVDAAEVDMI VGSLAGPLCA GGGFCAGSNE
IVKHQRITAT AYTFSAALPA MLATTASETI GLLQSTPEII IQLRENIKAM RTQLDPRSDW
VFCTSSTESP LMLLALKPSV VVSKNLSIGD QESLLQDIVD ETLVNGVLIT RLKSVPADLN
STPRDPNWYQ QPALKVCITT GLSKKEIERA GVTIRHAITK VMNKRK
//
