ID J9EST4_WUCBA Unreviewed; 396 AA.
AC J9EST4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=WUBG_10773 {ECO:0000313|EMBL:EJW78319.1};
OS Wuchereria bancrofti.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX NCBI_TaxID=6293 {ECO:0000313|EMBL:EJW78319.1, ECO:0000313|Proteomes:UP000004810};
RN [1] {ECO:0000313|Proteomes:UP000004810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA {ECO:0000313|Proteomes:UP000004810};
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Hepburn T.,
RA Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Wuchereria bancrofti.";
RL Submitted (AUG-2012) 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, 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:EJW78319.1}.
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DR EMBL; ADBV01006712; EJW78319.1; -; Genomic_DNA.
DR AlphaFoldDB; J9EST4; -.
DR Proteomes; UP000004810; 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 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; 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 PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 2.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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}.
FT MOD_RES 220
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 396 AA; 45297 MW; 639186BD96A4EE75 CRC64;
MTNWLAKALE LPEEFLNTEN GSGIGIIQNT ASDATYLAIL AARGRAVERI KVSEGIIGQE
LQVISDGTGE LCYYSYHDAT IITKLVAYCS DQAHSSVEKG VMLAAMRLRK LKTIRGGPFD
NFSVTAETLE KAIMTDRQNG LVPFIFIMTL GTTSSCGMDP VDKLGPICKR ENIWIHIDSA
YAGKSFKFEF SIGAFLLCPE FRYLSHGFEY IDSFNMNAHK ALPINFDCSP MWFRDGKQIL
KYFAVNPIYL KYDDQTCAVD YRHFQIALGR RFRSLKVWFV LRNFGISGLQ KHLRKMVDLA
KNFEALIQED QLLELFVPRT FGMVCFRLKD STNEMNEELN RRINDDRRIH LVASAVHGIY
FLRFAVCSIL TTYEDIKQAY LIIHNFAKDV RRDMKK
//
