PDXAL_PSEAE
ID PDXAL_PSEAE Reviewed; 337 AA.
AC Q9I1Q5;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative 4-hydroxythreonine-4-phosphate dehydrogenase 2 {ECO:0000250|UniProtKB:P19624};
DE EC=1.1.1.262 {ECO:0000250|UniProtKB:P19624};
DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase 2 {ECO:0000250|UniProtKB:P19624};
GN OrderedLocusNames=PA2212;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P19624};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P19624};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P19624};
CC Note=Binds 1 divalent metal cation per subunit. Can use ions such as
CC Zn(2+), Mg(2+) or Co(2+). {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG05600.1; -; Genomic_DNA.
DR PIR; C83370; C83370.
DR RefSeq; NP_250902.1; NC_002516.2.
DR RefSeq; WP_003113700.1; NZ_QZGE01000014.1.
DR AlphaFoldDB; Q9I1Q5; -.
DR SMR; Q9I1Q5; -.
DR STRING; 287.DR97_6218; -.
DR PaxDb; Q9I1Q5; -.
DR DNASU; 881915; -.
DR EnsemblBacteria; AAG05600; AAG05600; PA2212.
DR GeneID; 881915; -.
DR KEGG; pae:PA2212; -.
DR PATRIC; fig|208964.12.peg.2316; -.
DR PseudoCAP; PA2212; -.
DR HOGENOM; CLU_040168_0_1_6; -.
DR InParanoid; Q9I1Q5; -.
DR OMA; CGREEID; -.
DR PhylomeDB; Q9I1Q5; -.
DR BioCyc; PAER208964:G1FZ6-2252-MON; -.
DR UniPathway; UPA00244; UER00312.
DR Proteomes; UP000002438; 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.
PE 3: Inferred from homology;
KW Cobalt; Cytoplasm; Magnesium; Metal-binding; NAD; NADP; Oxidoreductase;
KW Pyridoxine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..337
FT /note="Putative 4-hydroxythreonine-4-phosphate
FT dehydrogenase 2"
FT /id="PRO_0000188816"
FT BINDING 173
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 274
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"
SQ SEQUENCE 337 AA; 36321 MW; 7F53FD3707265B13 CRC64;
MNAPSLPRLA MVLGDPAGIG PELIARLLAD TEVREKAHIV LIADEAEMRR GMRIAGCEFP
YRRIDALETL DFADATPLLH PWLSQGGDEF PRSEASAVGG RYSLETLALA LELTRSGRTD
AILFGPLNKT SLHMAGMDHS DELHWFAERL GFGGPFCEFN VLDDLWTSRV TSHVALAEVP
GLLSQERVGE AIRLIDDALR RSGLARPRIG VCGLNPHNGD NGSFGREELD IIAPAVQKAR
EQGIAADGPY PADTIFLKVQ GDARAFDAVV TMYHDQGQIA IKLMGFSRGV TVQGGLPIPI
ATPAHGTAFD IAGQGRADVG ATRQAFEIAC RMGRHKA
