Tag | Content |
---|
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 |
---|
253 | ADTLFQPKYLDNADA | acetylation | [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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |