PDXA_PROA2
ID PDXA_PROA2 Reviewed; 338 AA.
AC B4S6L0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000250|UniProtKB:P19624};
DE EC=1.1.1.262 {ECO:0000250|UniProtKB:P19624};
DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000250|UniProtKB:P19624};
GN Name=pdxA {ECO:0000250|UniProtKB:P19624}; OrderedLocusNames=Paes_0718;
OS Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=290512;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 271 / SK 413;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL Submitted (JUN-2008) 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:0000250|UniProtKB:P19624}.
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;
CC Evidence={ECO:0000250|UniProtKB:P19624};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P19624};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000250|UniProtKB:P19624};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
CC {ECO:0000250|UniProtKB:P19624}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P19624}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19624}.
CC -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC {ECO:0000250|UniProtKB:P19624}.
CC -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000305}.
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DR EMBL; CP001108; ACF45765.1; -; Genomic_DNA.
DR RefSeq; WP_012505302.1; NC_011059.1.
DR AlphaFoldDB; B4S6L0; -.
DR SMR; B4S6L0; -.
DR STRING; 290512.Paes_0718; -.
DR EnsemblBacteria; ACF45765; ACF45765; Paes_0718.
DR KEGG; paa:Paes_0718; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_0_10; -.
DR OMA; TAQVVMM; -.
DR OrthoDB; 1414545at2; -.
DR UniPathway; UPA00244; UER00312.
DR Proteomes; UP000002725; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005255; PdxA_fam.
DR PANTHER; PTHR30004; PTHR30004; 1.
DR Pfam; PF04166; PdxA; 1.
DR TIGRFAMs; TIGR00557; pdxA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; NAD; NADP; Oxidoreductase;
KW Pyridoxine biosynthesis; Reference proteome.
FT CHAIN 1..338
FT /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT /id="PRO_1000146492"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
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:0000250|UniProtKB:P19624"
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:0000250|UniProtKB:P19624"
FT BINDING 271
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
SQ SEQUENCE 338 AA; 36521 MW; B625A431436286D5 CRC64;
MKTTAWTIGD IHGIGPEIIL KTFDESLRST GQPEEKPIVI GSAEALLYYS KRLGLSIDIR
TIDAPEKAAA YPQGVLPVIS VGEPSSPLQP GTISAEAGRL SMLAIEKAAN LCLEGRCAAM
VTAPIHKEAV ARAGYPHTGH TDFLADLCAT DNPTMLFRDP VSGLMVALAT IHVALHRVPE
LIRSMDMSAF FSNLNRSLQS DFRIEQPRIA VLGLNPHASD GGVMGREEKE IILPCIDALA
DRQNIEGPFA ADGFFGSGKY RNYDVTVAMY HDQGLLPFKV LAFDTGINVT LGLPLVRTSP
DHGTSFDIAG QGRASHRSFS EAAKLAWEIA FNRLMEHS
