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Database: UniProt
Entry: A0A0B2D0T2_9PSED
LinkDB: A0A0B2D0T2_9PSED
Original site: A0A0B2D0T2_9PSED 
ID   A0A0B2D0T2_9PSED        Unreviewed;       330 AA.
AC   A0A0B2D0T2; A0A0B3BLT6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536};
DE            EC=1.1.1.262 {ECO:0000256|HAMAP-Rule:MF_00536};
DE   AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536};
GN   Name=pdxA {ECO:0000256|HAMAP-Rule:MF_00536};
GN   ORFNames=PT85_16715 {ECO:0000313|EMBL:KHO63590.1}, SAMN05421672_11425
GN   {ECO:0000313|EMBL:SIR07189.1};
OS   Pseudomonas flexibilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=706570 {ECO:0000313|EMBL:KHO63590.1, ECO:0000313|Proteomes:UP000030980};
RN   [1] {ECO:0000313|EMBL:KHO63590.1, ECO:0000313|Proteomes:UP000030980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14085 {ECO:0000313|EMBL:KHO63590.1,
RC   ECO:0000313|Proteomes:UP000030980};
RA   Shin S.-K., Yi H.;
RT   "Genome sequence of Pseudomonas tuomuerensis JCM 14085.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SIR07189.1, ECO:0000313|Proteomes:UP000186079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29606 {ECO:0000313|EMBL:SIR07189.1,
RC   ECO:0000313|Proteomes:UP000186079};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-
CC       threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which
CC       spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate
CC       (AHAP). {ECO:0000256|HAMAP-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:0000256|HAMAP-
CC         Rule:MF_00536};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
CC       Note=Binds 1 divalent metal cation per subunit. Can use ions such as
CC       Zn(2+), Mg(2+) or Co(2+). {ECO:0000256|HAMAP-Rule:MF_00536};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
CC       {ECO:0000256|HAMAP-Rule:MF_00536}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00536}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536}.
CC   -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC       {ECO:0000256|HAMAP-Rule:MF_00536}.
CC   -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00536}.
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DR   EMBL; JTAK01000009; KHO63590.1; -; Genomic_DNA.
DR   EMBL; FTMC01000014; SIR07189.1; -; Genomic_DNA.
DR   RefSeq; WP_039562622.1; NZ_JTAK01000009.1.
DR   AlphaFoldDB; A0A0B2D0T2; -.
DR   STRING; 706570.PT85_16715; -.
DR   PATRIC; fig|706570.3.peg.3163; -.
DR   OrthoDB; 9801783at2; -.
DR   UniPathway; UPA00244; UER00312.
DR   Proteomes; UP000030980; Unassembled WGS sequence.
DR   Proteomes; UP000186079; Unassembled WGS sequence.
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   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   HAMAP; MF_00536; PdxA; 1.
DR   InterPro; IPR037510; PdxA.
DR   InterPro; IPR005255; PdxA_fam.
DR   NCBIfam; TIGR00557; pdxA; 1.
DR   PANTHER; PTHR30004; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR30004:SF5; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF04166; PdxA; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00536};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00536}; NAD {ECO:0000256|HAMAP-Rule:MF_00536};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00536}; Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030980};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00536}.
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         166
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         211
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         266
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
SQ   SEQUENCE   330 AA;  35268 MW;  1C8408AA50B5DAA3 CRC64;
     MSCRLFALTP GEPAGIGPDL CLLLSREAQP HALVSIASRE LLRQRAGELG LEITLLDVGP
     GRWPQEPAPA GSLYVWHTPL QSPAQPGRLD PANAGYVLET LRRAGEGCVA GTFAGMITAP
     VHKGVINEGG VPFSGHTEFL AELTHTEQVV MMLATEGLRV ALVTTHLPLK DVAAAITPER
     LTRVTRILHA DLRDKFGIAR PRILVCGLNP HAGEGGHLGR EEIEVIEPTL EQLRQEGMDL
     VGPLPADTLF TPKHLEHCDA VLAMYHDQGL PVLKYKGFGA AVNVTLGLPI IRTSVDHGTA
     LDLAGSGRID TGSLRVALHT AYLMADSRPC
//
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