ID D0SL43_ACIJU Unreviewed; 322 AA.
AC D0SL43;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 67.
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 ECO:0000313|EMBL:EEY92750.1};
GN ORFNames=HMPREF0026_00026 {ECO:0000313|EMBL:EEY92750.1};
OS Acinetobacter junii SH205.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=575587 {ECO:0000313|EMBL:EEY92750.1, ECO:0000313|Proteomes:UP000018442};
RN [1] {ECO:0000313|Proteomes:UP000018442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH205 {ECO:0000313|Proteomes:UP000018442};
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
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; GG705011; EEY92750.1; -; Genomic_DNA.
DR RefSeq; WP_005402062.1; NZ_GG705011.1.
DR AlphaFoldDB; D0SL43; -.
DR HOGENOM; CLU_040168_2_0_6; -.
DR UniPathway; UPA00244; UER00312.
DR Proteomes; UP000018442; 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 Zinc {ECO:0000256|HAMAP-Rule:MF_00536}.
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT BINDING 161
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 206
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 261
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 269
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
SQ SEQUENCE 322 AA; 34926 MW; E5A8706F5FB8D890 CRC64;
MLPLYVTSGE PAGIGPDICL NLANRQDLRP VVVLADIDML KQRIEQLGLE VELVLYSGQT
EPSLNGQLYV EHIALAKPVI LGCLDAENAS YVLEQLHRSA DYALSGKSVG VATAPVQKSI
INDAGIVFSG HTEYYQEFAH VDRVVMMLAT KTLRVALATT HLPLRDVPDA ITQERLHQVI
DILIHDLKTK FKINQPRILV CGLNPHAGED GYLGREEIDV INPVLEEYRA QGVKMSLSLP
ADTLFTSENL KDADAVLAMY HDQGLPVLKS QGFGEAVNIT LGLPFIRTSV DHGTALSLAG
TGQAKASSLH VAVDLALDLA RD
//