(data stored in ACNUC7421 zone)

SWISSPROT: PDXA_ECO57

ID   PDXA_ECO57              Reviewed;         329 AA.
AC   P58713;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 1.
DT   05-JUL-2017, entry version 105.
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=Z0061, ECs0057;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG54357.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33480.1; -; Genomic_DNA.
DR   PIR; A85487; A85487.
DR   PIR; A90636; A90636.
DR   RefSeq; NP_308084.1; NC_002695.1.
DR   RefSeq; WP_000241259.1; NZ_MWVM01000003.1.
DR   ProteinModelPortal; P58713; -.
DR   SMR; P58713; -.
DR   STRING; 155864.Z0061; -.
DR   EnsemblBacteria; AAG54357; AAG54357; Z0061.
DR   EnsemblBacteria; BAB33480; BAB33480; BAB33480.
DR   GeneID; 913457; -.
DR   KEGG; ece:Z0061; -.
DR   KEGG; ecs:ECs0057; -.
DR   PATRIC; fig|386585.9.peg.156; -.
DR   eggNOG; ENOG4105CEZ; Bacteria.
DR   eggNOG; COG1995; LUCA.
DR   HOGENOM; HOG000221592; -.
DR   KO; K00097; -.
DR   UniPathway; UPA00244; UER00312.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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; P58713.
DR   SWISS-2DPAGE; P58713.
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_0000188806.
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;  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
//

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