ID   PDXAL_NOVAR             Reviewed;         330 AA.
AC   O85987;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Putative 4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000250|UniProtKB:P19624};
DE            EC=1.1.1.262 {ECO:0000250|UniProtKB:P19624};
DE   AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000250|UniProtKB:P19624};
OS   Novosphingobium aromaticivorans (Sphingomonas aromaticivorans).
OG   Plasmid pNL1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=48935;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700278 / DSM 12444 / F199;
RA   Romine M.F., Stillwell L.C., Wong K.-K., Thurston S.J., Sisk E.C.,
RA   Sensen C.W., Gaasterland T., Saffer J.D., Fredrickson J.K.;
RT   "Complete sequence of a 184 kb catabolic plasmid from Sphingomonas
RT   aromaticivorans strain F199.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-
CC       threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which
CC       spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate
CC       (AHAP). {ECO:0000250|UniProtKB:P19624}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl
CC         phosphate + CO2 + NADH; Xref=Rhea:RHEA:32275, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57279, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58452; EC=1.1.1.262;
CC         Evidence={ECO:0000250|UniProtKB:P19624};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P19624};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P19624};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000250|UniProtKB:P19624};
CC       Note=Binds 1 divalent metal cation per subunit. Can use ions such as
CC       Zn(2+), Mg(2+) or Co(2+). {ECO:0000250|UniProtKB:P19624};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
CC       {ECO:0000250|UniProtKB:P19624}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P19624}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19624}.
CC   -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC       {ECO:0000250|UniProtKB:P19624}.
CC   -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000305}.
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DR   EMBL; AF079317; AAD04003.1; -; Genomic_DNA.
DR   PIR; T31279; T31279.
DR   RefSeq; NP_049207.1; NC_002033.1.
DR   RefSeq; WP_010891025.1; NC_002033.1.
DR   AlphaFoldDB; O85987; -.
DR   SMR; O85987; -.
DR   UniPathway; UPA00244; UER00312.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005255; PdxA_fam.
DR   PANTHER; PTHR30004; PTHR30004; 1.
DR   Pfam; PF04166; PdxA; 1.
PE   3: Inferred from homology;
KW   Cobalt; Cytoplasm; Magnesium; Metal-binding; NAD; NADP; Oxidoreductase;
KW   Plasmid; Pyridoxine biosynthesis; Zinc.
FT   CHAIN           1..330
FT                   /note="Putative 4-hydroxythreonine-4-phosphate
FT                   dehydrogenase"
FT                   /id="PRO_0000188830"
FT   BINDING         169
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         213
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         263
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
SQ   SEQUENCE   330 AA;  34579 MW;  55ABBF8B500CE707 CRC64;
     MSTASERVRP VVGTMIGDPA GIGPEVAVRA LADGAVHTDS IPVLVGSAAA VERALDFTGT
     KARLRVMRGF EKPSDDPAII DVIDTGALPD GVLPLGEDTE AAGHATAQWL DELDALARDG
     SFAATIMGPI STGSLKLAKK LDRVISPTPG ESYLVLLTGP LRVAHLTDHM SLRQVIDVIS
     ADLVATAVGQ LHEAMQSWGI AQPRIAVAGL NPHAMGDEDR LEIAPGIEAA RARGIDVEGP
     IAPDSVFRHC IEGRYDMVLA MFHDQGHIAV KTWGFSGNSV IIMGPPYLHM SVAHGTAYDI
     VGTGKADAAM MLSAMRTCGR LASGRGFEQA