ID A0A199VI03_ANACO Unreviewed; 1801 AA.
AC A0A199VI03;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=ACMD2_23367 {ECO:0000313|EMBL:OAY76767.1};
OS Ananas comosus (Pineapple) (Ananas ananas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC Bromelioideae; Ananas.
OX NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY76767.1, ECO:0000313|Proteomes:UP000092600};
RN [1] {ECO:0000313|EMBL:OAY76767.1, ECO:0000313|Proteomes:UP000092600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY76767.1};
RX PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA Redwan R.M., Saidin A., Kumar S.V.;
RT "The draft genome of MD-2 pineapple using hybrid error correction of long
RT reads.";
RL DNA Res. 0:0-0(2016).
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:OAY76767.1}.
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DR EMBL; LSRQ01001727; OAY76767.1; -; Genomic_DNA.
DR STRING; 4615.A0A199VI03; -.
DR Proteomes; UP000092600; 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 InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR PANTHER; PTHR12741:SF7; CALLOSE SYNTHASE 12; 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:UP000092600};
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 332..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 404..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 579..598
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1367..1389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1449..1468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1513..1532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1538..1560
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1644..1665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1677..1698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1705..1729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1749..1767
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 180..296
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1801 AA; 207293 MW; 837965B95EAF9A87 CRC64;
MSLRQRPVPG AAGNGPRRGP GGGGGGAAEA EAEAEAYNII PIHNVLADHP SLRFPEVRAA
MAALRTVGDL RTPPFVPWHD GLDLLDWLGA FFGFQRDNVR NQREHLVLLL ANAQMRLQPP
PDNIEALDPA VVRRLRKKLL HNYTSWCAFL GRKPNVWVSD SPSPASLLRR PSSSSSADPR
RDLLYISLYL LIWGEAANLR FVPECLAYIF HHMAMDLNRI LEGYTDDATG RPALPAISGE
NAFLARVVVP VYKTISAEVA ASRNGTAPHT AWRNYDDVNE YFWSRHVFDR LRWPLDLSRG
FFAAPPSRNR VGKTGFVEQR SFWNVYRSFD RLWVMLLLFL QAAAIVAWQG HLWPWRNLRT
RDDQVPVLTV FITWAALRLL QAMLDAGTQY SLVSRENRWL ALRMALKILV AAGWTVAFSV
LYARVWDQRH RDRGPGWSRA ADQRLLNFLE AAAVFVLPEV LALVLFLVPW LRNFLEKTNW
RILYVLTWWF QTRTFVGRGL REGLVDNVKY SLFWAVLLAA KFSFSYFLQI QPMVAPTKAI
YNIRRVNYQW HEFFAHANRF AAVVLWIPVV LIYLMDIQIW YAIFSSLTGA LVGLFSHLGE
IRNVQQLRLR FQFFASAMQF NLMPEEQLFK DRGTLRSKFK DAILRLKLRY GLGRPYKKIE
SNQVEARRFA LIWNEIIASF REEDVISDRE VELLELPPDL WNIRVVRWPC LLLCNELLLA
LGQAKELEAS DRRHWRKICK NEYRRCAVIE AYDSVRFLLL RIVGEGTEEH SIVNQIFLAF
DDSMRAEKFT AEYKMAVLPS IHAKLITLLE LMLKPKKDMT KVVNTLQTLY DIAIRDFPTS
KKSIEQLKQE GLVPLRPSAT GLLFENAVEL PGENDATFYR QVRRLHTILT SRDSMNNVPK
NIEARRRIAF FSNSLFMNMP RAPQVEKMLA FSVLTPYYNE EVLYDKTQLH SENEDGVSIL
FYLQKIYEDD WAYFLERMKR EGMVSEKELW EERLRDLRLW ASYRGQTLSR TVRGMMYYYK
ALKMLAFLDS ASEIDIKDGS RELASIGSFR QEVDSYGLGD ADRLPSSRNL SRASSGVSLL
FKGHEYGTAL MKYTYVVACQ IYGNQKAKKD SRAEEILYLM KKNEALRVAY VDEVHTGTDE
VAYYSVLVKY DQRLEREVEI YRVRLPGPLK LGEGKPENQN HALIFTRGDA VQTIDMNQDN
YFEEALKMRN LLEEYNHYYG ARKPTLLGVR EHVFTGSVSS LAWFMSAQET SFVTLGQRVL
ANPLKVRMHY GHPDVFDRIW FLSRGGISKA SRVINISEDI FAGFNCTLRG GNVTHHEYIQ
VGKGRDVGLN QISMFEAKVA SGNGEQTLSR DVYRLGHRLD FFRMLSFFYT TVGFYFNTMM
VVLTVYAFVW GRLYLALSGL EKTITDSADS TNNKALGVVL NQQFIIQLGL FTALPMIVEN
SLEHGFLPAL WDFLTMQLQL ASVFFTFSMG TKTHYYGRTI LHGGAKYRAT GRGFVVQHKS
FAENYRLYAR SHFIKAIELG VILTVYASYS AIASDTLVYI VMTISSWFLV VSWIMAPFAF
NPSGFDWLKT VYDFDDFMSW IWYRGGIFAK PEQSWEVWWY EEQAHLRTTG LWGRLMEIVL
DLRFFFFQYG IVYQLKIASG SHSIAVYLLS WICVFAAVGV FVVMAYARDR YAAKEHIYYR
AVQAFIIILI VLVIIVLLKF TDFHIIDIFT SLLAFIPTGW GLISIAQVIR PFIESTVVWD
TVVAVARLYD ILFGVVVMAP VALLSWLPGF QEMQTRILFN EAFSRGLQIS RIITGKKPNA
I
//
