ID A0A2G5DJC3_AQUCA Unreviewed; 1777 AA.
AC A0A2G5DJC3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=AQUCO_01900181v1 {ECO:0000313|EMBL:PIA43604.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA43604.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA43604.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) 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}.
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DR EMBL; KZ305036; PIA43604.1; -; Genomic_DNA.
DR Proteomes; UP000230069; 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: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 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:UP000230069};
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..529
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 670..692
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 744..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1495..1517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1581..1599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1641..1659
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1665..1688
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 289..405
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1777 AA; 204796 MW; EF67A6E04ED74034 CRC64;
MANLDGLPPG LTRRPSRSAA TTTFSLEVFD NEVVPSSLQS IVPILRVATE IENERPRVAY
LCRFYAFEKA HRLDPSSTGR GVRQFKTALL QRLERDNASS LASRVKKSDA REIESFYQQY
YEHYVRALDR GEQADRAQLG KAYQTAGVLF EVLCAVNKSE KVEEVAPEII AAAKDVQEKK
DIYTPYNILP LDAAGASQCI MQFEEIKATV SALRNTHGLN WPTAFEQHKQ KTGDLDLLDW
LRAMFGFQLD DRAVDLIMSK MFKNYKTWCK FLGRKHSLRL PQGQHEVQQR KILYMGLYLL
IWGEAANIRF MPECLCYVFH NMAYELHGLL AGNVSIVTGE NIKPSYGGDD EAFLRKVVTP
LYRVLEKEAK KAGHGKAPHS AWCNYDDLNE YFWSPDCFSL GWPMRDDGDF FKSTRELKSA
KQGTRKKSES TGKSYFVETR TFWHIFRSFD RLWTFYILAL QIQRLVLYFI CSKFSKKKLA
GFLVDVRGKE YAFRETVKQH ILRTLMRPIL LIKIAFIYLK QFIISSFLFA CHFTFTFSCT
RSSILELLLN FPGYHRWKFT DVLRTLLKIV VSLAWAIILP ICYLHSLNNA PEKVKEVMNL
LRQVEGIPPL YAMVVILYLL PNLLAAVLFI FPMLRRWIEN SDWHIVRFLL WWSQPRIYIG
RGMHESQFSL IKYTLFWVLL LCSKLAFSYF IMIKPLIQPT KDIMSLQRVQ YTWHEFFPNA
KHNIGAVVSL WAPVIMVYFM DSQIWYSIFS TIYGGISGAF SRLGEIRTLG MLRSRFQSLP
GAFNAYLVPT EKTRKRGFSF SKRFAEASAN RRTEAAKFAQ LWNEVICSFR EEDLISDRKG
LLMDLLLVPY TSDPSLKLIQ WPPFLLASKI PIALDMAAQF RAKDSDLWKR ICADEYLKCA
VIECYESFKL VLNVLVVGEN EKRIVGIIFK EIESNISKNT FLTNFRMAPL PALCKKFVEL
IGILKDANPS KRGTVVLLLQ DMLEVVTRDM MVNEIRELVE LGHGNKDKQL FAGADPKPAI
VFPPVATPHW EEQIKRLYLL LTVKESAIDV PTNLEARRRI TFFANSLFMD MPRAPKVSKM
LSFSVMTPYY SEETVYSKND LEMENEDGVS IIFYLQKIYP DEWNNFMERV NCKRESEVWE
NDETILQLRH WVSLRGQTLS RTVRGMMYYR RALKLQAFLD MATEKEILEG YKAVTATTEE
EKKSQRSLYA HLEAIADMKF TYVATCQNYG NQKRSGDRRA TDILNLMVNN PSLRVAYIDE
VEERDAGRVQ KVYYSVLVKA ADKIDQEIYR IKLPGTAKIG EGKPENQNHA IIFTRGKALQ
TIDMNQDNYL EEALKMRNLL EEFHEDHGVR PPTILGVREH IFTGSVSSLA WFMSMQETSF
VTIGQRVLAN PLKIRFHYGH PDVFDRLFHI TRGGISKASQ GINLSEDIFA GFNSTLRRGN
VTHHEYIQVG KGRDVGLNQI SLFEAKVACG NGEQILSRDI YRLGHRFDMF RMLSCYFTTV
GFYISSVLVV LTVYFYLYGK LYLSLSGLEK SIIKFAKAKG KNPLQAAMAS QSVVQLGLLT
ALPMVMEIGL ERGFRTALGD FIIMNLQLAA VFFTFSLGTK VHYFGRTVMH GGAKYRATGR
GFVVRHEKFG ENYRMYSRSH FVKGLELMVL LVVYELYGSA ATDSISYVLL TGSIWFLVIS
WLFSPFLFNP SGFEWQKIVE DWDDWTKWIN SRGGIGVPAI KSWESWWAEE QEHLQYTGFL
GRFWEVVLSL RFFLYQYGIV YHLHIANGNT SIIVSSI
//