ID A0A2K5YFZ6_MANLE Unreviewed; 761 AA.
AC A0A2K5YFZ6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Pyridoxal dependent decarboxylase domain containing 1 {ECO:0000313|Ensembl:ENSMLEP00000014497.1};
GN Name=PDXDC1 {ECO:0000313|Ensembl:ENSMLEP00000014497.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000014497.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000014497.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR RefSeq; XP_011839042.1; XM_011983652.1.
DR AlphaFoldDB; A0A2K5YFZ6; -.
DR Ensembl; ENSMLET00000037946.1; ENSMLEP00000014497.1; ENSMLEG00000031146.1.
DR GeneID; 105542217; -.
DR CTD; 23042; -.
DR GeneTree; ENSGT00390000009628; -.
DR OMA; PEHSQYG; -.
DR OrthoDB; 3142408at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.170; -; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF1; PYRIDOXAL-DEPENDENT DECARBOXYLASE DOMAIN-CONTAINING PROTEIN 1-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT REGION 28..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 583..610
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 28..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 83741 MW; BF743BD1D9E5E562 CRC64;
MDASLEKIAD PTLAEMGKNL KEAMKMLEDS QRRTEEENGK KLISGDIPGP LQGRIQNIGE
QGHMALLGHS LGAYISTLDK EKLRKLTTRI LSDTTLWLCR IFRYENGCAY FHEEEREGLA
KICRLAIHSR YEDFVVDGFN VLYNKKPVIY LSAAARPGLG QYLCNQLGLP FPCLCRVPCN
TMFGSQHQMD VAFLEKMIKD DIERGRLPLL LVANAGTAAV GHTDKIGRLK ELCEQYGIWL
HVEGVNLATL ALGYVSSSVL AATKCDSMTM TPGPWLGLPA VPAVTLYKHD DPALTLVAGL
TSNKPADKLR ALPLWLSLQY LGLDGIVERI KHACQLSQRL QESLKKVNYI KILVEDELSS
PVVVFRFFQE LPDSDPVFKA VPVPTMTPSA VGRERHSCDA LNRWLGEQLK QLVPASGLTV
MDLEAEGTCV RFSPLMTAAV LGTRGEDVDQ LVACIESKLP VLSSTLQLRE EFKQEVEATA
GLLYVDDPNW PGIGVVRYEH ANDDKSSLKS DPEGEKIHAG LLKKLNELES DLTFKIGPEY
KSMKSCLYVG MASEDMDVAE LVETIAATAR EIEENSRLLE NMTEVVRKGI QEAQVELQKA
NEERLLEEGV LRQIPVVGSV LNWFSPVQAL QKGRTFNLTA GSLESTEPIY VYKAQGAGVT
PPPTPSGSRT KQRLPGQKPF KRSLRGSDAL SETSSASHIE DLEKVERLSG GLEQITLEAS
STEGHPGAPS PQHASQSEAF QKGAPHPEDD HPQVEGAESL R
//