ID A0A2K6E7E5_MACNE Unreviewed; 827 AA.
AC A0A2K6E7E5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Pyridoxal dependent decarboxylase domain containing 1 {ECO:0000313|Ensembl:ENSMNEP00000044077.1};
GN Name=PDXDC1 {ECO:0000313|Ensembl:ENSMNEP00000044077.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000044077.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000044077.1}
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 AlphaFoldDB; A0A2K6E7E5; -.
DR STRING; 9545.ENSMNEP00000044077; -.
DR Ensembl; ENSMNET00000068586.1; ENSMNEP00000044077.1; ENSMNEG00000044575.1.
DR GeneTree; ENSGT00390000009628; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000044575; Expressed in colon and 12 other cell types or tissues.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
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:UP000233120}.
FT REGION 28..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 610..637
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 741..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 91347 MW; C993631FF6CF9519 CRC64;
MDASLEKIAD PTLAEMGKNL KEAMKMLEDS QRRTEEENGK KLISGDIPGP LQGSGQDMVS
ILQLVQNLMH GDEDEEPQSP RIQNIGEQGH MALLGHSLGA YISTLDKEKL RKLTTRILSD
TILWLCRIFR YENGCAYFHE EEREGLAKIC RLAIHSRYED FVVDGFNVLY NKKPVIYLSA
AARPGLGQYL CNQLGLPFPC LCRVPCNTMF GSQHQMDVAF LEKMIKDDIE RGRLPLLLVA
NAGTAAVGHT DKIGRLKELC EQYGIWLHVE GVNLATLALG YVSSSVLAAT KCDSMTMTPG
PWLGLPAVPA VTLYKHDDPA LTLVAGLTSN KPADKLRALP LWLSLQYLGL DGIVERIKHA
CQLSQRLQES LKKVNYIKIL VEDELSSPVV VFRFFQELPD SDPVFKAVPV PTMTPSAVGR
ERHSCDALNR WLGEQLKQLV PASGLTVMDL EAEGTCVRFS PLMTAAVLGT RGEDVDQLVA
CIESKLPVLS STLQLREEFK QEVEATAGLL YVDDPNWPGI GVVRYEHAND DKSSLKSDPE
GEKIHAGLLK KLNELESDLT FKIGPEYKSM KSCLYVGMAS EDMDVAELVE TIAATAREIE
ENSRLLENMT EVVRKGIQEA QAELQKANEE RLLEEGVLRQ IPVVGSVLNW FSPVQALQKG
RTFNLTAGSL ESTEPIYVYK AQGAGVTPPP TPSGSRTKQR LPGQKPFKRS LRGSDALSET
SSASHIEDLE KVERLSGGPE QITLEASSTE GHPGAPSPQH ASRSEAFQKG APHPEDDHPQ
LLQLLLPWQL TWAQLRNTNQ QITLMLIQPG SLLKSVEARS HCLFLLF
//
