(data stored in ACNUC7421 zone)

SWISSPROT: PDXA_ECODH

ID   PDXA_ECODH              Reviewed;         329 AA.
AC   B1XC53;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 63.
DE   RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536};
DE            EC=1.1.1.262 {ECO:0000255|HAMAP-Rule:MF_00536};
DE   AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536};
GN   Name=pdxA {ECO:0000255|HAMAP-Rule:MF_00536};
GN   OrderedLocusNames=ECDH10B_0053;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(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). {ECO:0000255|HAMAP-
CC       Rule:MF_00536}.
CC   -!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + NAD(+) = 3-amino-
CC       2-oxopropyl phosphate + CO(2) + NADH.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00536};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00536};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00536};
CC       Note=Binds 1 divalent metal cation per subunit. Can use ions such
CC       as Zn(2+), Mg(2+) or Co(2+). {ECO:0000255|HAMAP-Rule:MF_00536};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00536}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00536}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00536}.
CC   -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC       {ECO:0000255|HAMAP-Rule:MF_00536}.
CC   -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00536}.
DR   EMBL; CP000948; ACB01257.1; -; Genomic_DNA.
DR   RefSeq; WP_000241277.1; NC_010473.1.
DR   ProteinModelPortal; B1XC53; -.
DR   SMR; B1XC53; -.
DR   EnsemblBacteria; ACB01257; ACB01257; ECDH10B_0053.
DR   KEGG; ecd:ECDH10B_0053; -.
DR   eggNOG; ENOG4105CEZ; Bacteria.
DR   eggNOG; COG1995; LUCA.
DR   HOGENOM; HOG000221592; -.
DR   KO; K00097; -.
DR   OMA; APVHKGV; -.
DR   UniPathway; UPA00244; UER00312.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00536; PdxA; 1.
DR   InterPro; IPR005255; PdxA.
DR   PANTHER; PTHR30004; PTHR30004; 1.
DR   Pfam; PF04166; PdxA; 1.
DR   TIGRFAMs; TIGR00557; pdxA; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1XC53.
DR   SWISS-2DPAGE; B1XC53.
KW   Cobalt; Cytoplasm; Magnesium; Metal-binding; NAD; NADP;
KW   Oxidoreductase; Pyridoxine biosynthesis; Zinc.
FT   CHAIN         1    329       4-hydroxythreonine-4-phosphate
FT                                dehydrogenase.
FT                                /FTId=PRO_1000128244.
FT   METAL       166    166       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00536}.
FT   METAL       211    211       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00536}.
FT   METAL       266    266       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_00536}.
FT   BINDING     136    136       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00536}.
FT   BINDING     137    137       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00536}.
FT   BINDING     274    274       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00536}.
FT   BINDING     283    283       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00536}.
FT   BINDING     292    292       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00536}.
SQ   SEQUENCE   329 AA;  35114 MW;  44E1FEE233C86233 CRC64;
     MVKTQRVVIT PGEPAGIGPD LVVQLAQREW PVELVVCADA TLLTNRAAML GLPLTLRPYS
     PNSPAQPQTA GTLTLLPVAL RAPVTAGQLA VENGHYVVET LARACDGCLN GEFAALITGP
     VHKGVINDAG IPFTGHTEFF EERSQAKKVV MMLATEELRV ALATTHLPLR DIADAITPAL
     LHEVIAILHH DLRTKFGIAE PRILVCGLNP HAGEGGHMGT EEIDTIIPVL NELRAQGMKL
     NGPLPADTLF QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA
     LELAGRGKAD VGSFITALNL AIKMIVNTQ
//

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