PDXD1_BOVIN
ID PDXD1_BOVIN Reviewed; 787 AA.
AC A7MBC2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Pyridoxal-dependent decarboxylase domain-containing protein 1;
DE EC=4.1.1.-;
GN Name=PDXDC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; BC151480; AAI51481.1; -; mRNA.
DR RefSeq; NP_001095329.1; NM_001101859.2.
DR AlphaFoldDB; A7MBC2; -.
DR SMR; A7MBC2; -.
DR STRING; 9913.ENSBTAP00000043763; -.
DR iPTMnet; A7MBC2; -.
DR PaxDb; A7MBC2; -.
DR PeptideAtlas; A7MBC2; -.
DR PRIDE; A7MBC2; -.
DR Ensembl; ENSBTAT00000046463; ENSBTAP00000043763; ENSBTAG00000004801.
DR GeneID; 505868; -.
DR KEGG; bta:505868; -.
DR CTD; 23042; -.
DR VEuPathDB; HostDB:ENSBTAG00000004801; -.
DR eggNOG; KOG0630; Eukaryota.
DR GeneTree; ENSGT00390000009628; -.
DR HOGENOM; CLU_014327_0_0_1; -.
DR InParanoid; A7MBC2; -.
DR OMA; RYCPLEL; -.
DR OrthoDB; 804210at2759; -.
DR TreeFam; TF313101; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000004801; Expressed in saliva-secreting gland and 107 other tissues.
DR ExpressionAtlas; A7MBC2; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Decarboxylase; Lyase; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..787
FT /note="Pyridoxal-dependent decarboxylase domain-containing
FT protein 1"
FT /id="PRO_0000311215"
FT REGION 29..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P996"
FT MOD_RES 688
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99K01"
FT MOD_RES 692
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P996"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P996"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P996"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P996"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99K01"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P996"
SQ SEQUENCE 787 AA; 86615 MW; 9303DF36A3167EDB CRC64;
MDASLEKKIA DPTLAEMGKN LKEAMKMLED SQRRTEEENG KKLLSGDIPG PLQGSGQDMV
SILQLVQNLM HGDEDEQPQS TRIQNIGEQG HISLLGHSLG AYISTLDKEK LRKLTTRILS
DTTLWLCRIF RYENGCAYFH EEEREGLAKI CRLAIHSRYE DFVVDGFNVL YNRKPVLYLS
AAARPGLGQY LCNQLGLPFP CLCRVPCNTV FGSQHQMDVA FLEKLIKDDI ERGKLPLLLV
ANAGTAAVGH TDKIGRLKEV CEQYGIWLHV EGVNLATLAL GYVSSSVLAA TKCDSMTLTP
GPWLGLPAVP AVTLYKHDDP ALTLVSGLTS NKPADKLRAL PLWLSLQYLG LDGIVERIKH
ACQLSQRLQE SLKKVNHIKI LVEDELSSPV VVFRFFQELP GSDPGLNAIP APSAAASAVG
RERHSCDALN RWLGEQLKQL VPMSGLTVMD LEVEGTCVRF SPLMTAAVLG TRGEDVDQLV
ACVQSKLPVL TCTLQLREEF KQEVEATAGL LYVDDPNWPG IGVVRYEHAN DDKSSLKLDP
EGEKIHAGLL KKLNELESDL TFKMGPEYKS MKSCIYIGMA SDDIDISELV ETIAVTAREI
EEDSRLLENM TEVVRKGIQE AQVQLQKANE ERLLEEGVLR QIPVVGSVLN WFSPVQASQK
GRTFNLTAGS LESTEHTYVY KVQGSGVTPP QTPTGTRTKQ RLPGQKPFKR SLRGSDAISE
TSSVGHIEDL EKMEQSSGGQ EASEANSHER HPEAPAPPEA EPPGALQDGA QGLQDDRPQV
EEPESLR