ID   A0A090LPG8_STRRB        Unreviewed;       774 AA.
AC   A0A090LPG8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=SRAE_2000472900 {ECO:0000313|EMBL:CEF70089.1,
GN   ECO:0000313|WBParaSite:SRAE_2000472900.1,
GN   ECO:0000313|WormBase:SRAE_2000472900};
OS   Strongyloides ratti (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF70089.1};
RN   [1] {ECO:0000313|EMBL:CEF70089.1, ECO:0000313|Proteomes:UP000035682}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC   ECO:0000313|WBParaSite:SRAE_2000472900.1}, and ED321 Heterogonic
RC   {ECO:0000313|EMBL:CEF70089.1};
RA   Martin A.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SRAE_2000472900.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (DEC-2020) to UniProtKB.
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; LN609529; CEF70089.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090LPG8; -.
DR   STRING; 34506.A0A090LPG8; -.
DR   EnsemblMetazoa; SRAE_2000472900.1; SRAE_2000472900.1; WBGene00264968.
DR   WBParaSite; SRAE_2000472900.1; SRAE_2000472900.1; WBGene00264968.
DR   WormBase; SRAE_2000472900; SRP00653; WBGene00264968; -.
DR   OrthoDB; 47798at2759; -.
DR   Proteomes; UP000035682; Chromosome X.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        200..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   MOD_RES         577
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   774 AA;  89960 MW;  913F97E6938389ED CRC64;
     MKLKIIFLFL FFISIIKIYN CNIIVKESLY LLARKNFSIE IANAIYENFN VTKGEVYEGS
     LCRAANYNVL SNNSITSLTP IYLIVEEESK YIQCQEEGLQ NFLIVHIYGR KNGSGIVRIE
     KFNRINLIFE LNNYDYYHVK KALILFKTLK NTLTLHYSGI KKIFIPKKSN PPYWIHLITG
     GKLKNNIENI DDITTNIISY FNFFLLISEL IISSTIIVIL IYCMKGKHKK KKVQLNKMIL
     ELKQANTLDI PNDKELIDPN DIKSYFYTIV NQVSKYIDNH IKESNNYDVV PEQKNIENLM
     VLEPYMGNNK INELFDELFK NIMPSISFPH HIKNYNLKPG TNISDVISSI FISYISLIGI
     DRIPKSTIKM IEQGVYNWFG KAIGLPETFL YKQNSFNTTV VDSLFQNDDG GGLILSNNIL
     ANLQVIYGAR KMKIMKILKN YEKKDNFDNY LDIQKKLIVY MNEDQLGNYE KLCNSIFIIC
     KGIPFSDKIE LCQACLTKQI EEDISDGYIP FLIISSFAST TLCSYDDLNE ISYVCEKFDI
     WLHVDATYGG FSLINSKIRK KALGIEKCNS LLICPDKFMI CSPEISILFS RNFQFIFENF
     NIKELQNPED KWLINTEDVK KFLSLKLWFV FKIYGIEKLR ERITKLIQDT NKLKELIKND
     NRLELYDFLS LGIVSFKVSG DSQTKSSIKT SQLIKFINEK RQIYVSEYDV NKNIKLIQLS
     VIHITKTSNI ITNHWGEIQD IIDEFFNTQL EIPSISSSQH FEKENIISED FSQQ
//