ID A0A192CZL8_9SPHN Unreviewed; 337 AA.
AC A0A192CZL8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=A9D12_00615 {ECO:0000313|EMBL:ANK11698.1};
OS Erythrobacter neustonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1112 {ECO:0000313|EMBL:ANK11698.1, ECO:0000313|Proteomes:UP000078263};
RN [1] {ECO:0000313|EMBL:ANK11698.1, ECO:0000313|Proteomes:UP000078263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9434 {ECO:0000313|EMBL:ANK11698.1,
RC ECO:0000313|Proteomes:UP000078263};
RA Shi X.-L., Wu Y.-H., Cheng H., Xu L., Zhang X.-Q., Wang C.-S., Xu X.-W.;
RT "Compelete Genome Sequence of Bacteriochlorophyll-Synthesizing Bacterium
RT Porphyrobacter neustonensis DSM 9434.";
RL Submitted (MAY-2016) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00536}.
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DR EMBL; CP016033; ANK11698.1; -; Genomic_DNA.
DR RefSeq; WP_068348664.1; NZ_CP016033.1.
DR AlphaFoldDB; A0A192CZL8; -.
DR STRING; 1112.A9D12_00615; -.
DR KEGG; pns:A9D12_00615; -.
DR OrthoDB; 9801783at2; -.
DR UniPathway; UPA00244; UER00312.
DR Proteomes; UP000078263; 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 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:UP000078263};
KW Zinc {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 337 AA; 34384 MW; 23671820677A6149 CRC64;
MNLSHAPLAI TLGDPAGIGP EVILGAWARL RAERRAPPAF VVGGAGLLRA AGEALRIDCP
VVPIATADEA AFACAAGLPV MAGLDVPYAP GQPTADGAQA ALASLQWGTR LARAGTAAGV
VTAPIAKAAL AAIGWDYPGQ TEYLADACGA PYRDAVMMLA GPSLRTVPLT VHVALAEVPT
LLSPGLIVHK ARIVAAGLTR DFGIPRPRLA IAALNPHAGE QGQFGDEEAR IIAPAIAELR
AEGIDATGPV PGDALFTPRA RQGYDAALCM YHDQALIPLK ALEFDEGVNV TLGLPIIRTS
PDHGTAFDIA GKGLADPGAM AAAILMAADM AMARHRG
//
