ID   PDXD1_DANRE             Reviewed;         751 AA.
AC   Q66HY8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Pyridoxal-dependent decarboxylase domain-containing protein 1;
DE            EC=4.1.1.-;
GN   Name=pdxdc1; ORFNames=zgc:92179;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2004) 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; BC081619; AAH81619.1; -; mRNA.
DR   RefSeq; NP_001004552.2; NM_001004552.1.
DR   AlphaFoldDB; Q66HY8; -.
DR   SMR; Q66HY8; -.
DR   STRING; 7955.ENSDARP00000118338; -.
DR   PaxDb; Q66HY8; -.
DR   GeneID; 447813; -.
DR   KEGG; dre:447813; -.
DR   CTD; 23042; -.
DR   ZFIN; ZDB-GENE-040912-16; pdxdc1.
DR   eggNOG; KOG0630; Eukaryota.
DR   InParanoid; Q66HY8; -.
DR   PhylomeDB; Q66HY8; -.
DR   PRO; PR:Q66HY8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..751
FT                   /note="Pyridoxal-dependent decarboxylase domain-containing
FT                   protein 1"
FT                   /id="PRO_0000297680"
FT   REGION          659..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..707
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..730
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   751 AA;  83141 MW;  A5E123C385AA4A86 CRC64;
     MGNHLSDAMK ILESGKLETE QGQEGRKMSW KEIPGPLQGD GQDVVSILQL VQNLMHGDDE
     EQGHRMQFVG EQGHMALLGH SLAAYISVLE RERLRKLTTR ILSDTTLWLC RLFRYENGSA
     YFHEDDREGL LKVCRLVMNT HYEDFTTEGF TALSSKHPVI YQSAACRPGL GQHLCSQLGL
     PLSCLCVVPC NTMFGSLHQM DVALLDKLVK DDRDSGKLPL LLIANAGTPG AGHTDKLSRL
     KELCVQYNMW LHVEGVNLAT LVLGQVSSTV TAATKCDSMT LTPGPWLGLP AVPAVTLYRH
     EDPALSLAAG LTSSQPVEKL RALPLWLSLQ YLGHDGIVER IKHASQLSQQ LLEHLKTLAS
     IKTSVEDELN SPVVVFRFSH ENSAPSSGGS VEGSYAGERD ILDAFNRWLG DQLAEQVPLS
     GVDVVELEDE GTCVRFSPLM TAAALGTQEN DVAALVEKLA EMIPLLCCTL RLRQDFRDEV
     LQQASLSYIE DLNWPGLGVV RFEPRTTDLD EDKRQDRVEK INSDLLKKLM ELDTDLNFSG
     GPEFSEEKNC IFIGIATEDL DVAELVETIM SLGRDIEESG KLFENMTEVV RKGIQEAELQ
     LQKANEEKLM EEGVLRQIPL VSSVLNWFSP VQASVKGRTF NLAEGCLDST EPVYSIKAQM
     RKEDSPDSPK ANTRRFPGQK LFRRPGAGSD SISETSSVSQ LEESFRETLH SQAADEAEVP
     QERPAHILEE TAIADQRVPE GQEAESVETI R