CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004789
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 4-hydroxythreonine-4-phosphate dehydrogenase 
Protein Synonyms/Alias
 4-(phosphohydroxy)-L-threonine dehydrogenase 
Gene Name
 pdxA 
Gene Synonyms/Alias
 b0052; JW0051 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
253ADTLFQPKYLDNADAacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Catalyzes the NAD(P)-dependent oxidation of 4- (phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4- (phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). 
Sequence Annotation
 METAL 166 166 Divalent metal cation; shared with
 METAL 211 211 Divalent metal cation; shared with
 METAL 266 266 Divalent metal cation; shared with
 BINDING 136 136 Substrate.
 BINDING 137 137 Substrate.
 BINDING 274 274 Substrate.
 BINDING 283 283 Substrate.
 BINDING 292 292 Substrate.  
Keyword
 3D-structure; Cobalt; Complete proteome; Cytoplasm; Magnesium; Metal-binding; NAD; NADP; Oxidoreductase; Pyridoxine biosynthesis; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 329 AA 
Protein Sequence
MVKTQRVVIT PGEPAGIGPD LVVQLAQREW PVELVVCADA TLLTNRAAML GLPLTLRPYS 60
PNSPAQPQTA GTLTLLPVAL RAPVTAGQLA VENGHYVVET LARACDGCLN GEFAALITGP 120
VHKGVINDAG IPFTGHTEFF EERSQAKKVV MMLATEELRV ALATTHLPLR DIADAITPAL 180
LHEVIAILHH DLRTKFGIAE PRILVCGLNP HAGEGGHMGT EEIDTIIPVL NELRAQGMKL 240
NGPLPADTLF QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA 300
LELAGRGKAD VGSFITALNL AIKMIVNTQ 329 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IDA:EcoCyc.
 GO:0050897; F:cobalt ion binding; IEA:HAMAP.
 GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
 GO:0051287; F:NAD binding; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IDA:EcoCyc.
 GO:0042823; P:pyridoxal phosphate biosynthetic process; IMP:EcoCyc.
 GO:0008615; P:pyridoxine biosynthetic process; IMP:EcoCyc. 
Interpro
 IPR024084; IsoPropMal-DH-like_dom.
 IPR005255; PdxA. 
Pfam
 PF04166; PdxA 
SMART
  
PROSITE
  
PRINTS