ID A0A2P5E6L7_TREOI Unreviewed; 1954 AA.
AC A0A2P5E6L7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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-glucan synthase {ECO:0000256|ARBA:ARBA00032165};
GN ORFNames=TorRG33x02_230500 {ECO:0000313|EMBL:PON81166.1};
OS Trema orientale (Charcoal tree) (Celtis orientalis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Trema.
OX NCBI_TaxID=63057 {ECO:0000313|EMBL:PON81166.1, ECO:0000313|Proteomes:UP000237000};
RN [1] {ECO:0000313|Proteomes:UP000237000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:PON81166.1}.
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DR EMBL; JXTC01000223; PON81166.1; -; Genomic_DNA.
DR STRING; 63057.A0A2P5E6L7; -.
DR InParanoid; A0A2P5E6L7; -.
DR OrthoDB; 211713at2759; -.
DR Proteomes; UP000237000; 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 GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.270; Vacuolar protein sorting-associated protein vta1; 1.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR InterPro; IPR039431; Vta1/CALS_N.
DR InterPro; IPR023175; Vta1/CALS_N_sf.
DR PANTHER; PTHR12741:SF70; CALLOSE SYNTHASE 2-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 Pfam; PF04652; Vta1; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000237000};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PON81166.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 477..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 506..527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 547..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 588..616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 652..673
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 702..721
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 726..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1520..1543
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1564..1585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1597..1618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1684..1708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1762..1780
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1792..1809
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1829..1850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1856..1875
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1896..1917
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 309..424
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1954 AA; 225224 MW; D19A3D2360DEA477 CRC64;
MAYNRRYDEP TQRLQRAQTA RNVLEPMLDS EVVPSSLVDI APILRVANEV EAENPRVAYL
CRFYAFEKAH RLDPKSSGRG VRQFKTALLQ RLEREDKTTL AGKVKSDARE MQNFYQNYYK
KYIQALHADK ADRSRLTRAY QTAKVLFEVL RAVNQTEAVP DEILEAHTKV EEKSQLYVPF
NILPLDPDSQ NHAIMRYPEI QAAVSALRNT RGLPWPKGYK KKIDEDILDW LMLMFGFQEH
NVANQREHLI LLLANVHMRQ WPKPDQSKLD DRALTDVMKK LFKNYKQWCK YLDRKSSLWL
PNIQQEVQQR KLLYMGLYLL IWGEAANLRF MPECLCYIYH HMAFELYGML AGSVSALTGE
HTKPAYGGEK EAFLKKVVTP IYNVIAKEAQ RSKGKSKHSQ WRNYDDLNEY FWSVDCFRLG
WPMRADAAFF CCPSEDLKVD RDNKETKRYT RDRWIGKTNF VEIRSFSHIF RSFDRMWSFY
ILCLQAMIIV AWNGSGKLGS IFEGDVFNKV LSIFITAAIL NLGQATLDII LSWKARRSMS
YYSQLRYALK AITAAAWVII LPVSYAYGLK NPSGFAQTMK NWFGKGPGSS SVFILAVVIY
LAPNMLSVLF FLFPFIRRPL ERSNNKILAL MMWWSQPRLY VGRGMHESFP SLFKYTMFWV
LLLVSKLAFS YYVEIRSLVG PTKAIMDVHI STYQWHEFFP HASNNIGVVI ALWAPIILVY
FMDTQIWYAI FSTIFGGIYG AFRRLGEIRT LVMLRSRFQS IPGAFNDCLI PKEKSEQIKK
KGLKAAFFRK YDEVLSKKEE AAKFAQLWNE IVSSFREEDL ISDREMNLLL VPYMADPDLD
IIQWPPFLLA SKIPIALDMA KDSSGKDSEL KKRISTDTYM LCAVRECYLS FKSIINILVQ
GDREKLVMKE IFSSIDELIK NGNLIAELNM SALPSLYDQS VELIKYLLEN RKEDKDQVAI
VLLNMLEIVS RDIMEDETPS LLESSHGGSY GNDEGMVPLD QQYKFFSALR FPVTSDTDAW
KEKIRRLHLL LTEKESAMDV PSNLEARRRM SFFSNSLFME MPPAPKVRNM LSFSVLTPYF
KEEVAFSIDL LEKENEDGVS ILFYLQKIFP DEWTNFLQRV KCTSEEQLRT SVELEEQLCL
WASYRGQTLT KTVRGMMYYR KALELQAFLD MAKDSDLMKG YKAAESNNAE LGERSLMVQC
QAVADMKFAY VVSCQQYGID KRAGVDRAKD ILNLMRTYPS LRVAYIDEVE EPITEDKSIE
ASKEKSIGTS KSKFKPKVQK VYYSKLVKVP AKRSDSSEPV QSLDQLIYQI KLPGPAILGE
GKPENQNHAI IFTRGEGLQT IDMNQDNYLE EAFKMRNLLQ ELLKKHGGVR EPTILGLREH
IFTGSVSSLA WFMSNQETSF VTIGQRLLAN PLKVRFHYGH PDVFDRLFHL TRGGVSKASK
IINLSEDIFA GFNSTLREGN VTHHEYIQVG KGRDVGLNQI SLFEAKIANG NGEQTLSRDI
YRLGHRFDFF RMLSCYVTTV GFYFSTLLSV LTVYVFLYGR LYLALSGLEE GLRTQPAIRD
NKSLQVALAS QSFVQIGLLM ALPMVMEIGL EKGFRNALTD FILMQLQLAP VFFTFSLGTK
THYYGRTLLH GGAEYRGTGR LFVVFHAKFA ENYRLYSRSH FVKGIELMIL LLVYHIFGHS
YRGVVAYVLI TVSMWFLVGT WLFAPFLFNP SGFEWQKIVD DWNDWNKWMS NQGGIGVSPD
KSWESWWEKE QEHLRHSGMR GAIVEILLAL RFFIYQYGLV YHLSITRKTK SFLVYGISLL
VMILVLLLMK VGSVGRRRFS AKFQLLFRLF KGLVFLSFLT IFITLIALPH MTLQDVVAII
LAFMPTGWGL LLIAQACKPL IVKTGLWGLV RTLARFFEII MGMLLFTPVA FLAWFPFVSE
FQTRMLFNQA FSRGLQISRI LGGPRKDRSS SRKE
//
