ID   PDXA_ECOHS              Reviewed;         329 AA.
AC   A7ZW04;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 12.
DE   RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase;
DE            EC=1.1.1.262;
DE   AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase;
GN   Name=pdxA; OrderedLocusNames=EcHS_A0058;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic
RT   analysis of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-
CC       (phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-
CC       (phosphohydroxy)butyric acid which spontaneously decarboxylates to
CC       form 3-amino-2-oxopropyl phosphate (AHAP) (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4-(phosphonooxy)-L-threonine + NAD(+) = (2S)-
CC       2-amino-3-oxo-4-phosphonooxybutanoate + NADH.
CC   -!- COFACTOR: Binds 1 divalent metal cation per subunit. Can use ions
CC       such as zinc, magnesium or cobalt (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 4/5.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: The active site is located at the dimer interface
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the pdxA family.
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DR   EMBL; CP000802; ABV04458.1; -; Genomic_DNA.
DR   RefSeq; YP_001456841.1; -.
DR   GeneID; 5592043; -.
DR   GenomeReviews; CP000802_GR; EcHS_A0058.
DR   KEGG; ecx:EcHS_A0058; -.
DR   OMA; A7ZW04; TTKRIAI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenas...; IEA:HAMAP.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00536; -; 1.
DR   InterPro; IPR005255; PyrdxlP_synth_PdxA.
DR   Pfam; PF04166; PdxA; 1.
DR   TIGRFAMs; TIGR00557; pdxA; 1.
PE   3: Inferred from homology;
KW   Cobalt; Complete proteome; Cytoplasm; Magnesium; Metal-binding; NAD;
KW   NADP; Oxidoreductase; Pyridoxine biosynthesis; Zinc.
FT   CHAIN         1    329       4-hydroxythreonine-4-phosphate
FT                                dehydrogenase.
FT                                /FTId=PRO_1000061031.
FT   METAL       166    166       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   METAL       211    211       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   METAL       266    266       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   BINDING     136    136       Substrate (By similarity).
FT   BINDING     137    137       Substrate (By similarity).
FT   BINDING     274    274       Substrate (By similarity).
FT   BINDING     283    283       Substrate (By similarity).
FT   BINDING     292    292       Substrate (By similarity).
SQ   SEQUENCE   329 AA;  35209 MW;  F732A738D82FE1EC CRC64;
     MVKTQRVVIT PGEPAGIGPD LVVQLAQREW PVELVVCADA TLLTDRAAML GLPLTLRPYS
     PNSPAQPQTT GTLTLLPVAL RESVTAGQLA IENGHYVVET LARACDGCLN GEFAALITGP
     VHKGVINDAG IPFTGHTEFF EERSQAKKVV MMLATEELRV ALATTHLPLR DIADAITPAL
     LHEVIAILHH DLRTKFGIAE PRILVCGLNP HAGEGGHMGT EEIDTIIPVL DELRAQGMKL
     NGPLPADTLF QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA
     LELAGRGEAD VGSFITALNL AIKMIVNTQ
//