PDXA_SALTY
ID PDXA_SALTY Reviewed; 329 AA.
AC P58717;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=STM0091;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH COBALT IONS,
RP COFACTOR, AND SUBUNIT.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of NAD-dependent dehydrogenase/carboxylase of Salmonella
RT typhimurium.";
RL Submitted (JAN-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}.
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DR EMBL; AE006468; AAL19055.1; -; Genomic_DNA.
DR RefSeq; NP_459096.1; NC_003197.2.
DR RefSeq; WP_000093016.1; NC_003197.2.
DR PDB; 1R8K; X-ray; 2.10 A; A/B=1-329.
DR PDBsum; 1R8K; -.
DR AlphaFoldDB; P58717; -.
DR SMR; P58717; -.
DR STRING; 99287.STM0091; -.
DR PaxDb; P58717; -.
DR DNASU; 1251609; -.
DR EnsemblBacteria; AAL19055; AAL19055; STM0091.
DR GeneID; 1251609; -.
DR KEGG; stm:STM0091; -.
DR PATRIC; fig|99287.12.peg.94; -.
DR HOGENOM; CLU_040168_1_0_6; -.
DR PhylomeDB; P58717; -.
DR BioCyc; SENT99287:STM0091-MON; -.
DR UniPathway; UPA00244; UER00312.
DR EvolutionaryTrace; P58717; -.
DR Proteomes; UP000001014; 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..329
FT /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT /id="PRO_0000188826"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 166
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 ECO:0000305|Ref.2"
FT BINDING 211
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 ECO:0000305|Ref.2"
FT BINDING 266
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 ECO:0000305|Ref.2"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:1R8K"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:1R8K"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1R8K"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 94..109
FT /evidence="ECO:0007829|PDB:1R8K"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:1R8K"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1R8K"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:1R8K"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 178..194
FT /evidence="ECO:0007829|PDB:1R8K"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:1R8K"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:1R8K"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:1R8K"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 266..277
FT /evidence="ECO:0007829|PDB:1R8K"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:1R8K"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1R8K"
FT TURN 301..306
FT /evidence="ECO:0007829|PDB:1R8K"
FT HELIX 312..327
FT /evidence="ECO:0007829|PDB:1R8K"
SQ SEQUENCE 329 AA; 34779 MW; 054D9F4E0F34E43B CRC64;
MSSAQRVVIT PGEPAGSGPD LVVQLAQRAW PIELVVCADG ALLTERAAML GLPLSLLPYS
PDVPAAPQPA GTLTLLPVSL RAPAISGQLT VENGPYVVET LARACDGCLN GEFAALITGP
VHKGVINDAG ISFTGHTEFF EERSQAKKVV MMLATEELRV ALATTHLPLR AIADAITPAL
LHEVIAILHH DLRTKFGIAE PRILVCGLNP HAGEGGHMGT EEIDTIIPVL DELRAQGMKL
NGPLPADTLF QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA
LELAGRGKAD VGSFITALNL AIKMIVNTQ
