ID A0A0T6BC19_9SCAR Unreviewed; 580 AA.
AC A0A0T6BC19;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 08-NOV-2023, entry version 25.
DE RecName: Full=Pyridoxal-dependent decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMK59_201 {ECO:0000313|EMBL:KRT84890.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT84890.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT84890.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT84890.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT84890.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) 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:KRT84890.1}.
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DR EMBL; LJIG01002050; KRT84890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6BC19; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000051574; 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 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 InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR11999:SF70; MIP05841P; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
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|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000051574}.
FT MOD_RES 305
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 580 AA; 65669 MW; B2F7C23737CFB349 CRC64;
MDLEEFRVRG KEMVDYICEY MNSLNKKRVT ADVEPCYLRN LLPSEAPEEP EDWDKIMDDV
NSKIMPGVTH WQHPRFHAYF PSGNSYPSIL GDMLSDAIGC IGFSWAASPA CTELETIVMD
WFGKAIGLPT DFITSTRGSR GGGVIQSSAS ECVLVSMLAA RNQAIKYLKK NNPHKDDIFF
LPKLVAYCSK EAHSCVEKAA MILLVKLRVL EPDENGSLRG ETLRKAMKDD EVLGLLPFFV
STTLGSTASC SFDNLPEIGP VCKKQPSTWL HVDGAYAGNS FICPELKYLM DGIEYADSFN
TNPNKWLLVN FDCSCLWVRD RMRLTGALVV DPLYLQHANS DETIDYRHWG IPLSRRFRSL
KMWFVIRKYG LSGLQKYIRN HIRLAKYFES LVKKDNRFEV VNDVKLGLVC FRLYGPDAVN
RNLLAKINVS GKLHMIPSMV KGKYIIRFCV VAENAVDADI EYAWSVVTTH ADEMMTKPVT
PDAIVRAPLT RQKSRRFSFT RSVSREIYKR TMSKSNLHDG ATPILIPDDE TDSPNNEEEQ
VVDVEVTTTN GYPDDDEVFA KDFNDFSITE SKITPKELAL
//