ID A0A443P3A2_9MAGN Unreviewed; 509 AA.
AC A0A443P3A2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Serine decarboxylase-like protein {ECO:0000313|EMBL:RWR85265.1};
GN ORFNames=CKAN_01411900 {ECO:0000313|EMBL:RWR85265.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR85265.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR85265.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR85265.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(2019).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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:RWR85265.1}.
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DR EMBL; QPKB01000005; RWR85265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443P3A2; -.
DR STRING; 337451.A0A443P3A2; -.
DR Proteomes; UP000283530; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR46101; -; 1.
DR PANTHER; PTHR46101:SF2; SERINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000283530}.
FT REGION 14..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 340
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 509 AA; 57138 MW; D81C76231D07A98F CRC64;
MAGGLQMLCN GDLNGKVESL PSPQEMSSES LSLVTENGGG GGGGGEVGRK EKREIVLGRN
VHMMCHAVTE PEADDEVTGE REAHMASVLA RYRKSLMERT KHHLGYPYNL DFDYGALAQL
QHFSINNLGD PFIESNYGVH SRQFEVGVLD WFAHLWELEK NEYWGYITNC GTEGNLHGIL
VGREVFPDGI LYASRESHYS VFKAAQMYRM QCVRVDALIS GEIDCADFRT KLLQNRDKPA
IVNVNIGLPP SFYSFLPLFL SMDSMLTIYI PSKFSGTTVK GAVDDLDLVI KTLEEIGYKH
DQFYIHCDGA LFGLMMPFVK LAPKVTFKKP IGSVSVSGHK FVGCPMPCGV QITRLEHINA
LSRNVEYLAS RDATIMGSRN GHAPIFLWYT LNRKGYRGFQ KEVQKCLHNA HYLKDRLQAE
GIGAMLNELS STVVFERPRD EEFVRRWQLA CQGNIAHVVV MPNVTVEKLD YFMNELIQKR
SSWFQDGKIL APCIATDIGQ ENCTCIQHS
//
