ID A0A445BX97_ARAHY Unreviewed; 1751 AA.
AC A0A445BX97;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
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_A08g039790 {ECO:0000313|EMBL:RYR43364.1};
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:RYR43364.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR43364.1, 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:RYR43364.1};
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:RYR43364.1}.
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DR EMBL; SDMP01000008; RYR43364.1; -; Genomic_DNA.
DR STRING; 3818.A0A445BX97; -.
DR OrthoDB; 904675at2759; -.
DR Proteomes; UP000289738; Chromosome a08.
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: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 286..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 515..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1320..1346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1366..1389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1401..1420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1489..1511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1595..1617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1629..1651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1663..1680
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1700..1718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..254
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1751 AA; 205305 MW; E26BA6E4A6A07CDC CRC64;
MTQSYETYNI IPIPNSNNSH PDQHPSLRYP EVIAASSALR SIGDLRLPPR WHPDMDLLDW
LSLFFGFQND NVRNQREHLL LQLANAQMRF SPAPDTVHHL HPSVLRSFRK KLLKNYKTWC
SFHGKKHHLK LINNHKKKTD NDLRLELLYV SLYLLIWGEA ANLRFIPECI CFIFHHMVKD
LNRILEDHDG KLPEVSGENA FLRLVVKPIY DIVKLEAESS RNGTAPHCDW MNYDDVNEIF
WNKSCFQKLK WPIDVGTSRF FLYRTGKTGF VERRSFWNLF RSFDRLWVML ILFLQASIIV
SWPGYKYPWK ALKRRRVQVR ILTVFITWSG LRLLQALLDF MMQGKVISKD TKRLGLRMFL
KFFVAAAWIL VFFRFYNLIW NEWDKEERKW SKKTNKVVMD FYMVAFVFLL PEILGFLFLL
FPWVSNFFEK RDWSILRLLS WWFHRTIYVG RGLREGLIDN IRYTLFWILV LTTKFTFSYF
LQIKPMIPLT KKILKLHVDI EWHDFFDHGK TDDKFALGLL WLPVILIYLM DIQIWYSIYS
SFVGAAVGLF AHLGEIRSMQ QVKLRFQFFA SAALFNLMPE EQSLNERGTF MSKIKDAMRR
MKLRYGFGQP YRKLESNHTE ANKFALIWNE IILSFREEDI ISDREVELLE LPKNLWNVRV
IRWPCVLLSN ELLLALSQAK ELANSSDKRL WRKICKDEFR RCAVLESYDC IKHLLLEIVI
KPGTEEHSIL ESLFQHIEKS IEIGKFTKSF KTTALPQLHS KLIKLIEVLS KRTLKDSTQM
VNILQALYEI TIREFLKEKR TAEKLISDGL APKHQSSANL LFENAVRLPE TTNENFYRQL
RRLHTILTSR DSMQKVPVNI MAKTRLAFFT NSLFMNMPHA PQVEKMKAFS VLTPYYSEEV
LYSKEQLRIE NEDGISILYY LQTIFDDEWK NFIERMRREG MENDDDIWTE KLMELRLWAS
YRGQTLSRTV RGMMYYYKAL KLLAFLDSAP DINVWDGSLN LSSMVKENKD GSDRVRSPFS
HCLSNAYTSE DLPFKGHDYG TASMKFTYVV ACQIYGAQKA KKDPRADEIL ALMKNNEALR
VAYVDEVSTS RDEKDYYSVL VKYDQEWERE VEIYRVKLPG PLKLGEGKPE NQNHAVIFTR
GDAVQTIDMN QDNYFEEALK IRNLLEEFNC YYGIRKPNIL GVREHIFTGS VSSLAWFMSA
QETSFVTLGQ RVLANPLKIR MHYGHPDVFD RFWFLTRGGL SKASRVINIS EDIFAGFNCT
LRGGNVTHHE YIQVGKGRDV GLNQISLFEA KVASGNGEQV LSRDVYRLGH RLDFFRMLSF
YYTTVGFFFN TMMVVLTVYA FLWGRLFLAL SGFEAAMQKK STNNKAFGAI LNQQFIIQLG
LFTALPMIVE NSLEHGFLQS MWDFLTMQLQ LSSVFFTFSM GTRCHFFGRT ILHGGAKYRA
TGRGFVVEHK SFAENYRLYA RSHFVKAIEL GLILIIYAQH SPVARNTVVY VIMTISSWFL
VSSWIIAPFL FNPSGFDWLK TVNDFDDFMD WIWYRGRVFA KAEESWEIWW YEEQDHLKVT
GFWGKVFEIV LDLRFFTFQY GTVYKLRITD GSTSISVYLL SWICVAVIFG IYVVLSFARN
KYEAKNHIYF RFVQSVIITL TIIVIVGLLN FTKFRFGDIF TSLLAFIPTG WGIILIAQVF
RPQLRRTRIW KGIVSLARLY DILFGVIVMA PVALFSWLPG CQSMQTRILF NEAFSRGLQI
FQIVTGKRTQ T
//
