ID A0A182JP03_9DIPT Unreviewed; 543 AA.
AC A0A182JP03;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Tyrosine decarboxylase {ECO:0008006|Google:ProtNLM};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR000237-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR000237-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR000237-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-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, 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 AlphaFoldDB; A0A182JP03; -.
DR STRING; 43041.A0A182JP03; -.
DR EnsemblMetazoa; ACHR000237-RA; ACHR000237-PA; ACHR000237.
DR VEuPathDB; VectorBase:ACHR000237; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000075881; 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; 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:SF177; MIP05841P; 1.
DR Pfam; PF00282; Pyridoxal_deC; 2.
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}.
FT REGION 490..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 543 AA; 60400 MW; 7A9B1695490B9CB1 CRC64;
KAIGLPDSFL ALKPGSRGGG VIQTSASECV LVTMLAARAQ AIKYLKQQHP FVEEGHLLSK
LMAYCSKEAH SCVEKAAMIS FVKLRILEPD EKCCLRADTL IKVRAEGTRR YTTRLNTGSR
PLSIYGGIAM EEDEQQGLIP FFVSTTLGTT GSCAFDDLAE IGEALQRFPS VWLHVDAAYA
GNAFICPELK YLLKGIQYAD SFNTNPNKWL LTNFDCSTLW VRDRIRLTSA LVVDPLYLQH
GYTDSAIDYR HWGVPLSRRF RSLKLWFVLR SYGISGLQAY IRHHIDLAKR FEALVLKDNR
FEVCNDVRLG LVCFRLKGTD RINEKLLSSI NASGKLHMVP ASVNDTYVIR FCAVAQNAKV
EDIDYAWDVI TDFASEILEK EQADEVSEIV DRRKTHTLAQ KRSFFVRMVS DPKIYNPAIN
KAQTPHRMST ELTSPGHDGT VVTVQSPKTP GSATWISWPL AFLFASADDG TKNDVTLRFR
HLDTMMRLSA SRRNSATGGS SPSPEGENGI TLLKSPKKSP ILMRKRGSSP NPPAVGTNNG
STK
//