PDXD1_XENLA
ID PDXD1_XENLA Reviewed; 782 AA.
AC Q6DF78;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Pyridoxal-dependent decarboxylase domain-containing protein 1;
DE EC=4.1.1.-;
GN Name=pdxdc1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-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; BC076864; AAH76864.1; -; mRNA.
DR RefSeq; NP_001086603.1; NM_001093134.1.
DR AlphaFoldDB; Q6DF78; -.
DR SMR; Q6DF78; -.
DR MaxQB; Q6DF78; -.
DR PRIDE; Q6DF78; -.
DR DNASU; 446438; -.
DR GeneID; 446438; -.
DR KEGG; xla:446438; -.
DR CTD; 446438; -.
DR Xenbase; XB-GENE-1005634; pdxdc1.L.
DR OMA; RYCPLEL; -.
DR OrthoDB; 804210at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 446438; Expressed in stomach and 19 other tissues.
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..782
FT /note="Pyridoxal-dependent decarboxylase domain-containing
FT protein 1"
FT /id="PRO_0000297679"
FT REGION 26..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 86206 MW; 8F55EFFE74A7EDCB CRC64;
MQKQIPQMVD PTLAEMGKNL DEAMKILEDN QRPSEEEKDG KKYTRKDIPG PLQGSGQNMV
SVLQLVQNLM HDDEEEQSPS LRRIQNVGEQ GHMALLGHSL AAYISVLDRE HLRKLTTRIL
SDTTLWLCRL FRYDNGSAYY HEDDREGLLK VCRLVIHSRY EDYTTDGFNV LYNKLPVIYI
SAASRPGLGQ SVCNQLGLPL SCLCRVPCNT MFGSQHEMDV ALLDRLIKDD IQSGKCPLLL
VANAGTPGAG HTDKLGRLKE LCDQYNIWLH VEGVNLATLA LGYVSSSVLA ATKCDSMTLT
LGPWLGLPAV PAVTLYRHED PSLSLAAGLT SSQPVEKLRA LPLWLSLQYL GHSGIVERIK
HASQLSQKLL ENLKNLSPVK TPVENDGSSP VVVFRFVYEG CKSDSTLNLS TIERDSDALN
QWLGDQLAAL VPSSGVDIVE LEDEGTCVRF NPLMTCAVLG TTAEDVEQLV ACLRMKIPVL
ENTLRLKEEF RQEVERIAGL SYINDYSWAG LGVLRYEQFS EEQDAAKREA DLEKITVALL
KKLNELETDL TFCSGPEFGA EKNCIYIGMA SEDLDVSELV ETITAMGREI EENSRLLENM
TEVVRKGILE AEVQLNKANE ERLLEEGVLR QIPLVGSMLN WLSPVQATPK GRTFNLTAGS
LETTEMTYIS KAQTTGLTPP PTPTSAHGKR QAGQKLFKRL SRNSDAMSET SSISHLEEVE
SLEALPMPEY DSSAAENSAM GEPFATAEQS STPSIVPTET SSEGSQEPSI PSANTAESDS
LR