ID V7BV14_PHAVU Unreviewed; 1752 AA.
AC V7BV14;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=PHAVU_005G103600g {ECO:0000313|EMBL:ESW21842.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW21842.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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; CM002292; ESW21842.1; -; Genomic_DNA.
DR RefSeq; XP_007149848.1; XM_007149786.1.
DR STRING; 3885.V7BV14; -.
DR EnsemblPlants; ESW21842; ESW21842; PHAVU_005G103600g.
DR GeneID; 18630671; -.
DR Gramene; ESW21842; ESW21842; PHAVU_005G103600g.
DR KEGG; pvu:PHAVU_005G103600g; -.
DR eggNOG; KOG0916; Eukaryota.
DR OMA; IDYAWHE; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000000226; Chromosome 5.
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 InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR PANTHER; PTHR12741:SF94; 1,3-BETA-GLUCAN SYNTHASE; 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 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:UP000000226};
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 285..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 400..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 514..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1320..1344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1364..1386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1398..1416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1487..1509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1560..1581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1593..1615
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1627..1647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1654..1677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1697..1716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..257
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1004..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1752 AA; 204939 MW; E3720196C5EDF998 CRC64;
MPNTRHHRHH VVHPYNILPL HNPTIDHPSL RFPEVRAAAA ALSSVGDLRL PPQWHPDMDL
LDWLGLLFGF QNDNVRNQRE HLLLHLANAQ MRLSPPQETL DAALLRSFRS KLLRNYTSWC
SYLAAKPAVN LSYRPANSSP SDQRRELLYV SLYLLIWGEA ANLRFLPECL SYIFHHMAKD
LNKFLQHHDY DNSLHQSSLH QPSFLDRVVQ PIYRILLSEV ESSRNGTVPH CEWRNYDDMN
EFFWDKRCFK KLKWPIDIGS GFFDKRVGKI GFVERRSFWN LFRSFHRLWV MLFLFLQAAL
IVAWEDKTYP WHALKDRDLQ VRVLTIFFTW SALRFFQSLL DIVMQWSRLV SVETIGLGLK
MILKAVVAAA WFVVFFIFYR KIWEQRRSDG NWSVEANKQL VNFLEIVFIF MIPELLALVF
LILPWVRNFI ENKDWCLFYV LSWWFQGRTF VGRGLSEGLM DNIRYTLFWA VVLASKFCFS
YFLQIRPMVP PSKMILDLKD VNYQWHELFQ NGNWFPLGLL WLPVILIYLM DIQIWYSIYS
SLVGVSVGLF AHLGEIRSMQ QLKLRFQFFA SAVLFNLMPE EQLLNARRTL SGKIKDAIHR
MKLRYGFGQP YMKLESNQSE ANKFALIWNE VIMCFREEDI ISDEEVELLE LPKNSWNVRV
IRWPCFLLCN ELLLALSQAK ELVDVSDKRL WRKMCKHEFR RCAVIETYDC IKHLLLQIIK
PNSEEHSIVM VLFQEIDHSL EIGKFTQVFK TTALPQLHNK LIKFVELLNK KQIDSSKIVN
TLQALYEIVV RDFFKEKRNI ERLREDGLAP QNPDSSEVLL FENAIQLPET INENFYRQIR
RLLTILTSRD SMQNVPVNLE ARRRITFFTN SLFMKMPHAP QVEKMMAFSV LTPYYSEEVV
YSKEQLRVGN EDGISTLYYL QTIYDDEWKN FMERMRREGM KNESDIWTHK LGDLRSWASY
RGQTLSRTVR GMMYYYKSLK LLAFLDSASE VEIREGTREL VSLNQDNSDG FSSNKSPPSP
MSLSTENSSA RLLFKGHDYG TASMKFTYVI SCQIYGAQKE RKDPRAEEIL YLMKNNEALR
VAYVDEVPFG SGEKEYYSVL AKYDQQLERE VEIYRVKLPG PIKLGEGKPE NQNHAIIFTR
GDAVQTIDMN QDNYFEEALK MRNLLEEYRY YYGIRKPTIL GMREHIFTAF VSSLAWFMSA
QEMSFVTLGQ RVLANPLKVR MHYGHPDVFD RFWFITRGGI SKASRVINIS EDIFAGFNCT
LRGGNVTHHE YIQVGKGRDV GLNQVSMFEA KVASGNGEQV LSRDVYRLGH KLDFFRMLSF
FYTTVGFFFN TMMVVLTVYA FLWGRLMLAL SGIEAAMVNH KNKALGIIVS QQFIVQIGIF
TALPMIVENS LEQGFLQAVW DFLTMQLQLS SVFYTFSMGT RSHFFGRTIL HGGAKYRATG
RGFVVEHKSF AENYRLYARS HFVKAIELGL ILIVYATQST VATDTFVYIV MTCSSWFLVA
SWILTPFMFN PSGFDWLKTV HDFHDFMNWI WNRQRVFAKA EQSWERWWYE EHDHLKLTGI
WGKLLEIILD LRFFIFQYGI VYRLGIAAGS TSIAVYFLSW IYVFVVFGIY VVVAYARNEY
EATQHMYFRL VQTLVIVIAI LVIVALLEFT KFKFMDIFTS LVAFIPTGWG MILIAQVFRP
FLQCTIVWNV VVSLARLYDI LFGIIVLTPV ALLSWLPGFQ PMQTRILFNE AFGRGLCIFQ
IVTGKKSSAK SH
//
