ID A0A3Q0ISP3_DIACI Unreviewed; 463 AA.
AC A0A3Q0ISP3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Alpha-methyldopa hypersensitive protein-like {ECO:0000313|RefSeq:XP_026679289.1};
GN Name=LOC108252376 {ECO:0000313|RefSeq:XP_026679289.1};
OS Diaphorina citri (Asian citrus psyllid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae;
OC Diaphorininae; Diaphorina.
OX NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_026679289.1};
RN [1] {ECO:0000313|RefSeq:XP_026679289.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_026679289.1; XM_026823488.1.
DR AlphaFoldDB; A0A3Q0ISP3; -.
DR STRING; 121845.A0A3Q0ISP3; -.
DR PaxDb; 121845-A0A3Q0ISP3; -.
DR KEGG; dci:108252376; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000079169; Unplaced.
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:SF60; 3,4-DIHYDROXYPHENYLACETALDEHYDE SYNTHASE; 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, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000079169}.
FT MOD_RES 151
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 463 AA; 51609 MW; 1BF8FC10B73F3C21 CRC64;
MVSILAAKRK KILDLTSAGP TVSENDIKSR LVAYASDQSN SSVEKSAIIG DVPVRQLRSD
DNGVLRGDAL LTAVKEDLAK GLIPCCLVAT LGTTGTCAFD NLEELGPICQ EYNIWLHVDA
AYAGSALLLP EYAHLKRGLE YVDSFAFNAH KWLLTNHDCS AMWVKNANHL TNTFFTDRVY
LKHTDAPMNT QSPDYTHWQT PLSRRFRALK LWMTLRSYGL KGLQAYLRKH ISLAKKFADL
VEKDDRFELV CPPSMGLVCF RLKGDNDLTN QLYERLMSHK QIYIIKASFQ GRPFLRFVVT
SPETNQCDVA FAWNEISHQS SEMNLPRGSS SVAKRNSTVV TKELTNGHAN SITILDGNPI
FTEIAKNSNE TPHGTYSSIP NGITHGHPTE IPNGSISHIL TNLHRVTLHG PELEHIGVDD
NLIYDTNDNE SSTKRKSNNK LEDLDAILSE KENVLRSSVI SIC
//
