PDXA_PSEAE
ID PDXA_PSEAE Reviewed; 328 AA.
AC Q9I5U4;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536};
DE EC=1.1.1.262 {ECO:0000255|HAMAP-Rule:MF_00536};
DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536};
GN Name=pdxA {ECO:0000255|HAMAP-Rule:MF_00536}; OrderedLocusNames=PA0593;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
RP COFACTOR, AND SUBUNIT.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of pyridoxal phosphate biosynthetic protein pdxA
RT PA0593.";
RL Submitted (APR-2005) to the PDB data bank.
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00536};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00536, ECO:0000269|Ref.2};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00536, ECO:0000269|Ref.2};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00536, ECO:0000269|Ref.2};
CC Note=Binds 1 divalent metal cation per subunit. Can probably use ions
CC such as Zn(2+), Mg(2+) or Co(2+). {ECO:0000255|HAMAP-Rule:MF_00536,
CC ECO:0000269|Ref.2};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
CC {ECO:0000255|HAMAP-Rule:MF_00536}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00536,
CC ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00536}.
CC -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC {ECO:0000255|HAMAP-Rule:MF_00536}.
CC -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000255|HAMAP-
CC Rule:MF_00536}.
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; AAG03982.1; -; Genomic_DNA.
DR PIR; A83572; A83572.
DR RefSeq; NP_249284.1; NC_002516.2.
DR RefSeq; WP_003109023.1; NZ_QZGE01000010.1.
DR PDB; 1YXO; X-ray; 2.01 A; A/B=1-328.
DR PDBsum; 1YXO; -.
DR AlphaFoldDB; Q9I5U4; -.
DR SMR; Q9I5U4; -.
DR STRING; 287.DR97_3562; -.
DR PaxDb; Q9I5U4; -.
DR PRIDE; Q9I5U4; -.
DR EnsemblBacteria; AAG03982; AAG03982; PA0593.
DR GeneID; 880733; -.
DR KEGG; pae:PA0593; -.
DR PATRIC; fig|208964.12.peg.629; -.
DR PseudoCAP; PA0593; -.
DR HOGENOM; CLU_040168_2_0_6; -.
DR InParanoid; Q9I5U4; -.
DR OMA; TAQVVMM; -.
DR PhylomeDB; Q9I5U4; -.
DR BioCyc; PAER208964:G1FZ6-600-MON; -.
DR UniPathway; UPA00244; UER00312.
DR EvolutionaryTrace; Q9I5U4; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_00536; PdxA; 1.
DR InterPro; IPR037510; PdxA.
DR InterPro; IPR005255; PdxA_fam.
DR PANTHER; PTHR30004; PTHR30004; 1.
DR Pfam; PF04166; PdxA; 1.
DR TIGRFAMs; TIGR00557; pdxA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalt; Cytoplasm; Magnesium; Metal-binding; NAD; NADP;
KW Oxidoreductase; Pyridoxine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..328
FT /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT /id="PRO_0000188815"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 165
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 210
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 265
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:1YXO"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:1YXO"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1YXO"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 93..108
FT /evidence="ECO:0007829|PDB:1YXO"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 135..142
FT /evidence="ECO:0007829|PDB:1YXO"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:1YXO"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 177..193
FT /evidence="ECO:0007829|PDB:1YXO"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:1YXO"
FT TURN 213..217
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:1YXO"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:1YXO"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:1YXO"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 265..276
FT /evidence="ECO:0007829|PDB:1YXO"
FT STRAND 281..289
FT /evidence="ECO:0007829|PDB:1YXO"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:1YXO"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:1YXO"
FT HELIX 311..326
FT /evidence="ECO:0007829|PDB:1YXO"
SQ SEQUENCE 328 AA; 34923 MW; 2C666738F21D7B8C CRC64;
MSLRFALTPG EPAGIGPDLC LLLARSAQPH PLIAIASRTL LQERAGQLGL AIDLKDVSPA
AWPERPAKAG QLYVWDTPLA APVRPGQLDR ANAAYVLETL TRAGQGCLDG HFAGMITAPV
HKGVINEAGI PFSGHTEFLA DLTHTAQVVM MLATRGLRVA LATTHLPLRE VADAISDERL
TRVARILHAD LRDKFGIAHP RILVCGLNPH AGEGGHLGRE EIEVIEPCLE RLRGEGLDLI
GPLPADTLFT PKHLEHCDAV LAMYHDQGLP VLKYKGFGAA VNVTLGLPII RTSVDHGTAL
DLAGSGRIDS GSLQVALETA YQMAASRC
