ID   CASL2_CANSA             Reviewed;         545 AA.
AC   A6P6W1;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Cannabidiolic acid synthase-like 2;
DE   Flags: Precursor;
GN   Name=CBDAS3;
OS   Cannabis sativa (Hemp) (Marijuana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Cannabis.
OX   NCBI_TaxID=3483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=17544411; DOI=10.1016/j.febslet.2007.05.043;
RA   Taura F., Sirikantaramas S., Shoyama Y., Yoshikai K., Shoyama Y.,
RA   Morimoto S.;
RT   "Cannabidiolic-acid synthase, the chemotype-determining enzyme in the
RT   fiber-type Cannabis sativa.";
RL   FEBS Lett. 581:2929-2934(2007).
CC   -!- FUNCTION: Has no cannabidiolic acid synthase activity.
CC       {ECO:0000269|PubMed:17544411}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q8GTB6};
CC       Note=Binds 1 FAD per subunit in a bicovalent manner.
CC       {ECO:0000250|UniProtKB:Q8GTB6};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- PTM: The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-
CC       N1-histidyl FAD linkage. {ECO:0000250|UniProtKB:Q8GTB6}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AB292684; BAF65035.1; -; mRNA.
DR   AlphaFoldDB; A6P6W1; -.
DR   SMR; A6P6W1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..545
FT                   /note="Cannabidiolic acid synthase-like 2"
FT                   /id="PRO_0000421146"
FT   DOMAIN          77..251
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   ACT_SITE        484
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         417
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        467
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        499
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        37..99
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        114..176
FT                   /note="6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-
FT                   Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GTB6"
SQ   SEQUENCE   545 AA;  62296 MW;  AD8B4E82A357F929 CRC64;
     MKCSTFCFWY VCKIIFFFLS FNIQISIANP QENFLKCLSQ YIPTNVTNAK LVYTQHDQFY
     MSILNSTVQN LRFTSDTTPK PLVITTPLNV SHIQGTILCS KKVGLQIRTR SGGHDAEGMS
     YISQVPFVIV DLRNMHSVKI DVHSQTAWVE SGATLGEVYY WINENNENLS FPAGYCPTVG
     TGGHFSGGGY GALMRNYGLA ADNIIDAHLV NVDGKVLDRK SMGEDLFWAI RGGGGENFGI
     IAAWKIRLVA VPSMSTIFSV KKNMEIHELV KLVNKWQNIA YMYEKELLLF THFITRNITD
     NQGKNKTTIH SYFSSIFHGG VDSLVDLMNK SFPELGIKKT DCKQLSWIDT IIFYSGVVNY
     NTTNFKKEIL LDRSGGRKAA FSIKLDYVKK PIPETAMVTI LEKLYEEDVG VGMFVFYPYG
     GIMDEISESA IPFPHRAGIT YEIWYIASWE KQEDNEKHIN WIRNVYNFTT PYVSQNPRMA
     YLNYRDLDLG KTNFESPNNY TQARIWGEKY FGKNFNRLVK VKTKVDPDNF FRNEQSIPPL
     PLRHH