ID   PDXA_AZOSB              Reviewed;         330 AA.
AC   A1K9J6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 18.
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=azo2885;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Azoarcus.
OX   NCBI_TaxID=62928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte
RT   Azoarcus sp. strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL95501.1; -; Genomic_DNA.
DR   RefSeq; YP_934388.1; -.
DR   GeneID; 4609107; -.
DR   GenomeReviews; AM406670_GR; azo2885.
DR   KEGG; azo:azo2885; -.
DR   OMA; A1K9J6; HAGEDGC.
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    330       4-hydroxythreonine-4-phosphate
FT                                dehydrogenase.
FT                                /FTId=PRO_1000051489.
FT   METAL       163    163       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   METAL       208    208       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   METAL       263    263       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   BINDING     133    133       Substrate (By similarity).
FT   BINDING     134    134       Substrate (By similarity).
FT   BINDING     271    271       Substrate (By similarity).
FT   BINDING     280    280       Substrate (By similarity).
FT   BINDING     289    289       Substrate (By similarity).
SQ   SEQUENCE   330 AA;  33928 MW;  6479DC89D6006E5C CRC64;
     MAALPVLAVT SGEPAGVGPE LCARLLARDW PARLVVLGDA DLIAARAAAV GSPIAVRHYS
     RGQAQAAGVL EVLHIPLAEP SDAGRLAVGN ARYVLALLDR ALAGCVGGEF AGMVTAPVHK
     GVICESGIAF SGHTEYLAEH TATPLVVMML VGGGMRVALA TTHLPLAAVS AAITRPVLEQ
     TLRILHADLV QRFGIAAPRI LVAGLNPHAG EGGHMGREEI EVITPVLDRL RAEGLQLVGP
     LPADTLFAPH TLAHGDAVLA MYHDQGLPVL KHASFGGGVN VTLGLPVIRT SVDHGTALDL
     AGSGRADPGS LYAAVELAVS MAEARARQPR
//