ID   PDXA_SYNFM              Reviewed;         345 AA.
AC   A0LIN6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
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=Sfum_1601;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000478; ABK17288.1; -; Genomic_DNA.
DR   RefSeq; YP_845723.1; -.
DR   GeneID; 4460101; -.
DR   GenomeReviews; CP000478_GR; Sfum_1601.
DR   KEGG; sfu:Sfum_1601; -.
DR   NMPDR; fig|335543.6.peg.1649; -.
DR   OMA; A0LIN6; MMLAGPS.
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    345       4-hydroxythreonine-4-phosphate
FT                                dehydrogenase.
FT                                /FTId=PRO_1000051520.
FT   METAL       173    173       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   METAL       218    218       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   METAL       274    274       Divalent metal cation; shared with
FT                                dimeric partner (By similarity).
FT   BINDING     143    143       Substrate (By similarity).
FT   BINDING     144    144       Substrate (By similarity).
FT   BINDING     282    282       Substrate (By similarity).
FT   BINDING     291    291       Substrate (By similarity).
FT   BINDING     300    300       Substrate (By similarity).
SQ   SEQUENCE   345 AA;  36533 MW;  030A0107EA02ED92 CRC64;
     MSSSKPRIAL TMGDPCGVGP DVIAQALASP TLFECCTPIV VGDPSALQRS MALSGASKKV
     LVLREPAELP DDPGSDRIPL IAPVELSGRD IEHGRPTAAT CGAVVRYIES AVAFALAGQV
     RGVCTGPINK ARMHEHGFDF PGHTEFLQAL TGSRRVVMML AGPRLRVSLA TIHEALADVP
     ALLNVEMLRE VIRITAEALI RDFGLQAPRL AVAGLNPHAG EEGRFGREEI EILRPAIESL
     RPPGRCTVTG PYPADTLFQR AHAGEFDAVV AMYHDQGLVP IKLVHFYDAV NVSLGLPIVR
     TSVDHGTAYD LAGTGRAHPG SLTAAVQLAA LMAHNRFAAV SPVVP
//