ID A0A239DSA1_9PROT Unreviewed; 340 AA.
AC A0A239DSA1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN05880556_10433 {ECO:0000313|EMBL:SNS34808.1};
OS Azospirillum sp. RU38E.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=1907313 {ECO:0000313|EMBL:SNS34808.1, ECO:0000313|Proteomes:UP000198368};
RN [1] {ECO:0000313|EMBL:SNS34808.1, ECO:0000313|Proteomes:UP000198368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU38E {ECO:0000313|EMBL:SNS34808.1,
RC ECO:0000313|Proteomes:UP000198368};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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; FZOI01000004; SNS34808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239DSA1; -.
DR OrthoDB; 9801783at2; -.
DR UniPathway; UPA00244; UER00312.
DR Proteomes; UP000198368; 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:SF6; D-THREONATE 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:UP000198368};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00536}.
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT BINDING 172
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 217
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 272
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 280
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
SQ SEQUENCE 340 AA; 35121 MW; 5F3C6F92C9629D7E CRC64;
MVTAPLGLTM GEPAGIGGDI ALMTWAGRQG RPVPPFVMLD DPQRLAALAE RLGLSVPVRV
VAEGELGSVA SLFADALPVL PVPLSHPVQL GRPDPANGAA VIASIDRAVD LSRRGLLAGV
VTNPIQKSAL YATGFRWPGH TEYLAHLAGL PDDGTVMLLE GGGLRVVLAT IHLALKDVAA
HLTADAILHV ARVTDAALRR DFGIASPRLA VAALNPHAGE GGAMGREEME IIAPAVAALQ
AEGINAKGPF PADTLFHAGA RADYDVVVCM YHDQGLIPLK TLDFDQGVNI TLGLPFVRTS
PDHGTALSLA GTGKASPTSL IAALHAARSI ASRRLGLSCD
//
