(data stored in ACNUC7421 zone)

SWISSPROT: PDXA_SHISS

ID   PDXA_SHISS              Reviewed;         329 AA.
AC   Q3Z5V7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 88.
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=SSON_0060;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-
CC       (phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-
CC       (phosphooxy)butyric acid which spontaneously decarboxylates to
CC       form 3-amino-2-oxopropyl phosphate (AHAP). {ECO:0000255|HAMAP-
CC       Rule:MF_00536}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl
CC         phosphate + CO2 + NADH; Xref=Rhea:RHEA:32275, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57279, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58452; EC=1.1.1.262; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00536};
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; CP000038; AAZ86855.1; -; Genomic_DNA.
DR   SMR; Q3Z5V7; -.
DR   EnsemblBacteria; AAZ86855; AAZ86855; SSON_0060.
DR   KEGG; ssn:SSON_0060; -.
DR   HOGENOM; HOG000221592; -.
DR   KO; K00097; -.
DR   OMA; HKGVINE; -.
DR   BioCyc; SSON300269:G1GL2-69-MONOMER; -.
DR   UniPathway; UPA00244; UER00312.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00536; PdxA; 1.
DR   InterPro; IPR037510; PdxA.
DR   InterPro; IPR005255; PdxA_fam.
DR   PANTHER; PTHR30004; PTHR30004; 1.
DR   Pfam; PF04166; PdxA; 1.
DR   TIGRFAMs; TIGR00557; pdxA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3Z5V7.
DR   SWISS-2DPAGE; Q3Z5V7.
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_1000051518.
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;  35178 MW;  B700A93F4791010E CRC64;
     MVKTQRVVIT PGEPAGIGPD LVVQLAQREW PVELVVCADA TLLTDRAAML GLPLTLRPYS
     PNSPAQPQTA GTLTLLPVAL RESVTAGQLA IENGHYVVET LARACDGCLN GEFAALITGP
     VHKGVINDAG IPFTGHTEFF EERSQAKKVV MMLATEELRV ALATTHLPLR DIADAITPAL
     LHEVIAILHH DLRTKFGIAE PRILVCGLNP HAGEGGHMGT EEIDTIIPVL NELRAQGMKL
     NGPLPADTLF QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA
     LELAGRGEAD VGSFITALNL AIKMIVNTQ
//

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