ID   A0A0M8ZRE3_9HYME        Unreviewed;      1244 AA.
AC   A0A0M8ZRE3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:KOX68436.1};
GN   ORFNames=WN51_03922 {ECO:0000313|EMBL:KOX68436.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX68436.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX68436.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX68436.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX68436.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533}.
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DR   EMBL; KQ435922; KOX68436.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8ZRE3; -.
DR   STRING; 166423.A0A0M8ZRE3; -.
DR   OrthoDB; 47798at2759; -.
DR   Proteomes; UP000053105; 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   CDD; cd06450; DOPA_deC_like; 2.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
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:SF177; MIP05841P; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 2.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 2.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053105}.
FT   REGION          617..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..644
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         996
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   1244 AA;  139507 MW;  41CDE7398336C914 CRC64;
     MFHLTNSNQS ILTKVNLFFV EHRCLKIVAM DIEEFRMRGK EMVEYICEFM SNIHNRRVTP
     DVGPGYLRPL LPSEAPQEPE SWEDIMRDVE SKIMPGITHW QHPRFHAYFP AGNSFPSILG
     DMLSDAIGCI GFSWAASPAC TELETIVCDW FGKAIGLPTD FLYFSSGSKG GGVIQGSASE
     CILVCMLAAR AQAIARLKES AAHAHLDETA LLGKLMAYCS RESHSCVEKD AMICFVKLRI
     LEPDEKSVLR GETLRQAIEA DVAEGYIPFF VSITLGTTAC CSFDNLREIG PVCKKYSGVW
     LHVDAAYAGN SFICPELKYL MAGIEYADSF NTNTNKFLLT NFDCSCLWVR DRFKLTGALV
     VDPLYLQHTH ADTAIDYRHW SIPLSRRFRS LKLWFVMRSY GISGLQAYIR NHVQLAKRFE
     ALVRKDARFE LCNEVVLGLV CFRAKGTDKL NQKLLSTIND SGKLHMVPAR VNQRFTIRFA
     LAAPNATASD VDIAWSIITD YLAELLESKD VMDELADIRE KKRKATLEQR RSFFVRMVSD
     PAIQPGFTKT PNRTGAKLDA QATIGGIGSN PTNTATLSDV RRSWISWPLA YLRKDTADTS
     ELSLRFRHLD TMVRLKASGT GSRRGSSNGC SPDPSPSASP SRGRSPNGRA MLDTAKKDFE
     STETVDPRTM EGVLENAQKI LNNAYADFGP SLDRYKCMVR GKEMIEYICE YLRTLEGKRV
     TANVDPGYLR PLLPKEAPAK GEPWDAIMRD VDSKIMPGIT HWQHPRFHAY FPAGNSFPSI
     LGDMLSDAIG CIGFSWAASP ACTELETIVL DWYAKAIDLP PEFLAEHKTS KGGGVIQGSA
     SECILVTMLA ARTQAIRTLK EQDPNTEDSA FLPRLVAYCS TEAHSCAEKA AMISLVKLRV
     LEPDEKGSLR GKRLESAIRE DVANGLVPFF VSTTLGTTGS CAFDNLVEIG PVCKLYPNIW
     LHVDGAYAGN AFICPEMRPL MAGIEHADSF NTNPNKWLLV NFDCSCLWVR DRVKLTSALV
     VDPLYLQHAR SGESIDYRHW GIPLSRRFRA LKLWFVMRSY GITGLQKYIR NHIRLARRFE
     TLMRRDKRFE ITNDVRVGLV CFRLKESDEI NQELLANINA SGRLHMIPAR VMGKYILRFC
     VIKENATDDD IDYAVDVIEE HATEVMLAHY EGTEDEFRAK GPKSPAALDK KLVRKFSFTR
     SVTRDVYKRS ISKSSLHDGA TPIMVVDDNS QVDTIEEDVF CNSR
//