ID A0A444Y118_ARAHY Unreviewed; 1894 AA.
AC A0A444Y118;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=Ahy_B08g090958 {ECO:0000313|EMBL:RYQ95607.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ95607.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYQ95607.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYQ95607.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) 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:RYQ95607.1}.
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DR EMBL; SDMP01000018; RYQ95607.1; -; Genomic_DNA.
DR Proteomes; UP000289738; Chromosome b08.
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:SF66; 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; 2.
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:UP000289738};
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 488..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..544
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..627
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 675..693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1460..1483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1503..1525
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1537..1558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1624..1648
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1702..1720
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1732..1749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1769..1789
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1796..1816
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1836..1857
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 318..434
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1894 AA; 218003 MW; 30ACAE3D05F95DDE CRC64;
MSYSRRGSDP PPQRRILRTQ TAGNLGADPI LDSEVVPSSL VEIAPILRVA NEVEASNPRV
AYLCRFYAFE KAHRLDPTSS GRGVRQFKTA LLQRLEREND TTLQGRVKSD AREMQNFYQH
YYKKYIQALQ NAADKDRAQL TKAYQTAAVL FEVLKAVNQT EAVDVAEEIL EAHTKVEENK
QLYAPYNILP LDPESGKEAI MRYPEIQAAV SALRNIRGLP WPKGHGDKNK LNQDILDWLQ
LMFGFQKGNV ENQREHLILL LANVHIRQVP RPDQPPKLDD RALTEVMKKL FRNYKKWCKY
LGRKSSLWLP TIQQEVQQRK LLYMGLYLLI WGEAANLRFM PECLCYIYHH MAFELYGILA
GSVSQLTGEP VKPAYGGDNE AFLMKVVKPI YDTIAKEALR SNTGKAKHSQ WRNYDDLNEY
FWSIDCFRLG WPMRIDSEFF YVSPLPEKRS ANKDEETGNI ARGRWIGKTN FVEIRSYWHV
FRSFDRMWSF YILCLQAMII IAWNGSGDLS SIFDGEVFKK ILSIFITAAI LKLAQAILDV
VLSWKARKVM SLHVKLRYIC KVISAAAWVV VLPVTYAFSW KNPSGFAQTI KNWFGNGSGS
PSLFILAIFL YLSPNILSAL LFVFPFIRRY LERSNNGIVK LMMWWSQIKP LVGPTKVIMQ
AHVSLYKWHE FFPHAKSNIG VVIAIWSPII LVYFMDTQIW YAIFSTIVGG IYGAFRRLGE
IRTLELLRSR FESIPGAFNA CLIPVEKSEK TKRKSLWATF FRKFEQVSSN KEKEAARFAQ
LWNKIITSLR EEDLIDNRII NFMLKSICMS IYIEQIPIAV SMAKDSFGKG QELEKRLTRD
KYMKSAVLEC YASFRNIINF LVLAEREKLV INNIFVIVDE HIKNGDLLTE LNMSALPNNK
QEDKDQVVIL LLDMLEIVTR DIMEGEVEGL LDSSHGGSFG KDERMTPLDQ QYQVFGRLAF
PVKTETEAWK EKIKRLHLLL TVKESAMDVP SNLDARRRIS FFSNSLFMDM PPAPKVRNML
SFSVLTPYYD EAVLFSIDEL EEPNEDGVSI LFYLQKIFPD EWKNFLERVE CKSEEQVRGE
LEEELRLWAS YRGQTLTKTV RGMMYIRQAL ELQAFLDMAK DDDLMKGYKA AELESKENPH
TERSLWTQCQ SLADMKFAYV VSCQQYGIHK RSGDPRAKEI LKLMTKYPSL RIAYVDEVEE
PSKDKTKKNE KVYYSALVKA ALPAKSIGSS ETVQSLDQVI YKIKLPGPAI LGEGKPENQN
HAIIFTRGEG LQTIDMNQDN YMEEAFKMRN LLQEFLKNHG VRQPTILGLR EHIFTGSVSS
LAWFMSNQEN SFVTIGQRLL ANPLKVRFHY GHPDVFDRLF HLTRGGISKA SKVINLSEDI
FAGMYFKFCM CFNSTLREGN VTHHEYIQVG KGRDVGLNQI SMFEAKIANG NGEQTMSRDI
YRLGHRFDFF RMLSCYFTTI GFYFSTLVTV LTVYVFLYGR LYLALSGLEE GLNNKRIIRD
NRALQAALTS QSVVQIGFLL ALPMVMEIGL ERGFRQALSE FVLMQIQLAP VFFTFSLGTK
THYYGRTLLH GGAQYRGTGR GFVVFHAKFA DNYRLYSRSH FVKGIELMIL LVVYHIFGKS
YRGTVTYVLI TLTIWFMVAT WLFAPFLFNP SGFEWQKIID DWTDWHKWIS NRGGIGVPPE
KSWESWWEKE HEHLHHSGMR GIITEIILSL RFFLYQYGLV YHLSITNTTQ SVLVYGLSWL
IIFVILGLMK GVSVGRRRLS ADFQLLFRLI KGSIFLTFLA TFIILIAVAK MTIKDIVVCI
LAVMPTGWGL LLIAQACKPA IQHAAFWGSV RALARGYEII MGLLLFTPVA FLAWFPFVSE
FQTRMLFNQA FSRGLQISRI LGRQRRDRAA NNKE
//