ID   E2BTW1_HARSA            Unreviewed;       480 AA.
AC   E2BTW1;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000256|ARBA:ARBA00040968};
DE            EC=4.1.1.28 {ECO:0000256|ARBA:ARBA00038886};
DE   AltName: Full=DOPA decarboxylase {ECO:0000256|ARBA:ARBA00041275};
GN   ORFNames=EAI_11893 {ECO:0000313|EMBL:EFN80860.1};
OS   Harpegnathos saltator (Jerdon's jumping ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX   NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN   [1] {ECO:0000313|EMBL:EFN80860.1, ECO:0000313|Proteomes:UP000008237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN80860.1,
RC   ECO:0000313|Proteomes:UP000008237};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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}.
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DR   EMBL; GL450531; EFN80860.1; -; Genomic_DNA.
DR   RefSeq; XP_011145002.1; XM_011146700.2.
DR   AlphaFoldDB; E2BTW1; -.
DR   STRING; 610380.E2BTW1; -.
DR   EnsemblMetazoa; XM_011146700.3; XP_011145002.1; LOC105186470.
DR   GeneID; 105186470; -.
DR   KEGG; hst:105186470; -.
DR   InParanoid; E2BTW1; -.
DR   OMA; NPGFNWS; -.
DR   OrthoDB; 47798at2759; -.
DR   PhylomeDB; E2BTW1; -.
DR   Proteomes; UP000008237; 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   GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06450; DOPA_deC_like; 1.
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:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE 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   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:UP000008237}.
FT   MOD_RES         303
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   480 AA;  54610 MW;  E9992C030FDD780C CRC64;
     MDADNFKDFA KEMAEYITNY LENIRDRRVL PTVEPGYMKP LLPSEAPQDP EEWQNVMADI
     ERVIMPGVTH WHSPKFHAYF PTAQSYPAIV ADMLSGAIAC IGFSWIASPA CTELEVIMLD
     WLGKMIDLPK EFLACSGGKG GGVIQGTASE ATLVALLGAK AKKLKQVKEQ HPEWTNPEII
     DKLVAYCSCQ AHSSVERAGL FSGVKFRLLP IDDKYKLRGD VFAKAIQEDR EKGLIPFYAV
     ATLGTTVCCA FDRLDEIGVV ANRENIWLHV DAAYAGSAFI CPEYRYLMKG IELADSYNFN
     PHKWMLINFD CSVLWFKDPT YVINAFNVDP LYLKHDMQGS APDYRHWQIP LGRRFRSLKL
     WFVLRLYGVE NLQKFIRKHI AQAHEFEAFI LSDPRFEIIG EVIMGLVCFR LKGSNDLNEA
     LLKRINGAGN IHLVPSKIND TFFLRLSVCS RYSESKDIQY SWKEIKLRAN EVLEEQSVTK
//