ID   PLD_MICLT               Reviewed;         342 AA.
AC   Q76KC2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Pyridoxal 4-dehydrogenase;
DE            EC=1.1.1.107;
GN   Name=pld1;
OS   Microbacterium luteolum (Aureobacterium luteolum).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Microbacterium.
OX   NCBI_TaxID=69367;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18; 164-180;
RP   231-265 AND 285-301, CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=YK-1;
RX   PubMed=15226311; DOI=10.1074/jbc.m405344200;
RA   Yokochi N., Yoshikane Y., Trongpanich Y., Ohnishi K., Yagi T.;
RT   "Molecular cloning, expression, and properties of an unusual aldo-keto
RT   reductase family enzyme, pyridoxal 4-dehydrogenase, that catalyzes
RT   irreversible oxidation of pyridoxal.";
RL   J. Biol. Chem. 279:37377-37384(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + pyridoxal = 4-pyridoxolactone + H(+) + NADH;
CC         Xref=Rhea:RHEA:21336, ChEBI:CHEBI:15378, ChEBI:CHEBI:16871,
CC         ChEBI:CHEBI:17310, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.107;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13 mM for pyridoxal {ECO:0000269|PubMed:15226311};
CC         KM=0.41 mM for L-fucose {ECO:0000269|PubMed:15226311};
CC         KM=0.91 mM for D-arabinose {ECO:0000269|PubMed:15226311};
CC         KM=3.5 mM for L-xylose {ECO:0000269|PubMed:15226311};
CC         KM=0.042 uM for NAD with L-fucose as hydrogen donor
CC         {ECO:0000269|PubMed:15226311};
CC         KM=0.05 uM for NAD with pyridoxal as hydrogen donor
CC         {ECO:0000269|PubMed:15226311};
CC         KM=0.58 mM for NADP with L-fucose as hydrogen donor
CC         {ECO:0000269|PubMed:15226311};
CC       pH dependence:
CC         Optimum pH is 8.0 with pyridoxal as substrate (9.5 with L-fucose as
CC         substrate). {ECO:0000269|PubMed:15226311};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:15226311};
CC   -!- PATHWAY: Cofactor degradation; B6 vitamer degradation; 4-pyridoxate
CC       from pyridoxal: step 1/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; AB092836; BAC97800.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q76KC2; -.
DR   SMR; Q76KC2; -.
DR   BRENDA; 1.1.1.107; 7273.
DR   SABIO-RK; Q76KC2; -.
DR   UniPathway; UPA00192; UER00588.
DR   GO; GO:0050235; F:pyridoxal 4-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042820; P:vitamin B6 catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd19161; AKR_AKR15A1; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   InterPro; IPR044478; Pld1-like.
DR   PANTHER; PTHR42686; PTHR42686; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   SUPFAM; SSF51430; SSF51430; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:15226311"
FT   CHAIN           2..342
FT                   /note="Pyridoxal 4-dehydrogenase"
FT                   /id="PRO_0000124682"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        61
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        86
FT                   /evidence="ECO:0000250"
FT   BINDING         245..255
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   342 AA;  37890 MW;  CA32C4574A6C8789 CRC64;
     MHLKASEKRA LGRTGLTVTA LGLGTAPLGG LYAPVSRADA DALLEAGWDS GIRYFDSAPM
     YGYGRCEHLL GDMLREKPER AVISTKVGRL MTNERAGRTL PPAPPKNPLD SGWHNGLNFR
     EVFDYSYDGV MRSFDDSQQR LGFPEIDLLY VHDIGRVTHA DRHEFHWNAL TRGGGFRALT
     ELRAAGNIKG FGLGVNEWQI IRDALEEADL DCSLLAGRYS LLDQVSEKEF LPLAQKRGMA
     LVIAGVFNSG ILAAPRGGEQ KFDYADAPAE IIARTNRLHD ICDEYHVPLA AAAMQFPLRH
     EAVSSILIGV RSPEQIRQNV VWFEQSIPDE FWTTLRSEGL IS