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Database: UniProt
Entry: A0A2K5YFZ6_MANLE
LinkDB: A0A2K5YFZ6_MANLE
Original site: A0A2K5YFZ6_MANLE 
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
//
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