ID A0A199VGM8_ANACO Unreviewed; 513 AA.
AC A0A199VGM8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Tyrosine/DOPA decarboxylase 2 {ECO:0000313|EMBL:OAY76026.1};
GN ORFNames=ACMD2_23095 {ECO:0000313|EMBL:OAY76026.1};
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:OAY76026.1, ECO:0000313|Proteomes:UP000092600};
RN [1] {ECO:0000313|EMBL:OAY76026.1, 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:OAY76026.1};
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 -!- 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:OAY76026.1}.
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DR EMBL; LSRQ01001930; OAY76026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A199VGM8; -.
DR STRING; 4615.A0A199VGM8; -.
DR Proteomes; UP000092600; 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:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010977; Aromatic_deC.
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; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR11999:SF96; TYROSINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
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:UP000092600}.
FT MOD_RES 322
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 513 AA; 56064 MW; D34885C23F8C366F CRC64;
MGSLHSDVVL EANNNNGAFA ANNPLEPEEF RRQAHVMVDF LADYYRDVGS YPVRSQVEPG
YLSKVLPGSA PNQPEPLDAI LRDVREHIVP GLTHWQSPSY FAYFPSSGST AGFLGEMLST
GFNVVGFNWM SSPAATELES IVMDWLGGML ALPRPFLFSG GGGGVLQGTT CEAILCTLTA
ARDRMLGRIG REHIGRLVVY GSDQTHCALQ KAAQIAGIHP ANFRAVKTRR EDHFGLSPAE
LRRAADADEA AGLIPLFLCA TVGTTSSTAV DPLPGLCAAA AEKGMWVHVD AAYAGSACIC
PEFRGFIDGV EGADSFSLNA HKWFFTTLDC CCLWVKRPDA LVRALSTNPE YLRNKATESR
SVVDYKDWQI ALSRRFRALK LWMVLRSYGV ANLRNFLRGH VRMAKDFEAM VAADARFEVV
VPRYFAMVCF RLLLPSPNAA GAGGDETAAN ELNRRLLEAA NASGRVYMTH AVVGGVYLIR
FAVGATLTEE WHVRAAWKVV VEHAEELLKE LCV
//
