ID A0A1I8B4U1_MELHA Unreviewed; 820 AA.
AC A0A1I8B4U1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|WBParaSite:MhA1_Contig134.frz3.gene32};
OS Meloidogyne hapla (Root-knot nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC Meloidogyne.
OX NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig134.frz3.gene32};
RN [1] {ECO:0000313|WBParaSite:MhA1_Contig134.frz3.gene32}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533}.
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DR AlphaFoldDB; A0A1I8B4U1; -.
DR WBParaSite; MhA1_Contig134.frz3.gene32; MhA1_Contig134.frz3.gene32; MhA1_Contig134.frz3.gene32.
DR Proteomes; UP000095281; 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 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 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT REGION 46..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 92213 MW; FA632F0A6D186D0E CRC64;
MIREILVKVI EKPSPIVDPY FITSLEFLWV MECFEDDKLT QKLSFSSSTS TATPLPSSTS
GVPTSNFVPS PHGSITQMNK IEQLRDKINE ALIEGQNNRK RTAADQLLQQ IAEHFSKVNL
NDSRKGSSNV DDSCGSSRQR LGAAKSTAGM NAVEFRRRGR QMVDYITDYM ENIENRRVVP
SIEPGYLKEL LPLHAPQTAE PFERLLQDFE SYIMPGVTHW THPRFHAYFP AGNSFPSILA
DMLSDALGAI GFSWAACPAM TELEIHMLQW LGEMIGLPVA FLPFTENGTG GGVIQVITVN
ALIEAQSSAS ECNFVALLAA RFEIMKELRQ RFPFVEEGLL MSKLIAYCSK EAHSSVEKAA
MIAMIKLRIL ETDSSFRLRG ETLQTAVSED RNLGLIPFFV STTLGTTSCC SFDVLSEVGP
VCTHNGLWLH VDAAYAGSAM ICPEFRYLMA GIEHAMSFNT NPNKWMLVNR TSDYRHWGIP
LSRRFRSLKL WFVIRSYGIE GLQRYIREHV RLAKLFECLL LADDQLFEVV AEVLMGLVCF
RMKASDELNQ LLLTKLNSSG RIHMVPASLN DRFVIRFCVC YENATERDIQ IAYEIIKQTA
MSLREPIPEP IAENYELEME EAEQYDQMMQ DKQKNRNSPN IELNRNSSLR RQSIGSSSIN
TPSYPQQQQN LQQNIQQMGN SPLAIGIGSE QTIGGHSPSS LTSSTGADRR RLHTLAEKRS
FLVRMVSDPK CYNPKIVRHL NMRAHNQTSA ELFRDRTLRQ AIQQGSFQQR SSLGAGTSHG
RIGANAPFSS GKYACMSIDQ GSDEDDYQSL YFQNDQNLGI
//