ID D0LQB4_HALO1 Unreviewed; 338 AA.
AC D0LQB4;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 OrderedLocusNames=Hoch_6454 {ECO:0000313|EMBL:ACY18923.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY18923.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY18923.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(2010).
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=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000256|HAMAP-
CC 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; CP001804; ACY18923.1; -; Genomic_DNA.
DR RefSeq; WP_012831515.1; NC_013440.1.
DR AlphaFoldDB; D0LQB4; -.
DR STRING; 502025.Hoch_6454; -.
DR KEGG; hoh:Hoch_6454; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_1_0_7; -.
DR UniPathway; UPA00244; UER00312.
DR Proteomes; UP000001880; 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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000001880}.
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT BINDING 157
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 202
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 259
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 267
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
SQ SEQUENCE 338 AA; 34957 MW; 3AB59FA5A66D8AE9 CRC64;
MTTSDKIGIT LGDPAGIGPE IIAAAVADAS AELRGRLTLF GDRPILERAF AQITGSRIPS
DIQVVDRGLL SADQAIPGSP TGASGAAQVA YLEAAVSAAR RGTIGGLVTA PINKRSARQA
GFSFPGHTEF LAERLGAQHV AMMFAGPRLK VVLATVHLAL SEVPGALTRD GIVRTAKLAA
EAVSRDFGIA SARVGVLGLN PHAGEHGLFG REELEIIGPA IEECRRQIDG AQVDGPLIPD
AAFRQADGGA YDVLVAMYHD QGLIPVKLLD FEQAVNVTLG LPIVRTSPDH GVAYDIAGTG
KARPQSFMAA LSLAARLTTH RSASEASAGE PEDADSPS
//
