PDXA_CAMJE
ID PDXA_CAMJE Reviewed; 364 AA.
AC Q9PN58; Q0P917;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02086};
DE EC=1.1.1.262 {ECO:0000255|HAMAP-Rule:MF_02086};
DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02086};
GN Name=pdxA {ECO:0000255|HAMAP-Rule:MF_02086}; OrderedLocusNames=Cj1239;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2] {ECO:0007744|PDB:3TSN}
RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) IN COMPLEX WITH NICKEL.
RA Osipiuk J., Gu M., Kwon K., Anderson W.F., Joachimiak A.;
RT "4-hydroxythreonine-4-phosphate dehydrogenase from Campylobacter jejuni.";
RL Submitted (SEP-2011) 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_02086}.
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_02086};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02086};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02086};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02086};
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_02086}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02086}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02086}.
CC -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC {ECO:0000255|HAMAP-Rule:MF_02086}.
CC -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000255|HAMAP-
CC Rule:MF_02086}.
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; AL111168; CAL35354.1; -; Genomic_DNA.
DR PIR; A81331; A81331.
DR RefSeq; WP_002853162.1; NC_002163.1.
DR RefSeq; YP_002344630.1; NC_002163.1.
DR PDB; 3TSN; X-ray; 2.63 A; A/B/C/D=1-364.
DR PDBsum; 3TSN; -.
DR AlphaFoldDB; Q9PN58; -.
DR SMR; Q9PN58; -.
DR IntAct; Q9PN58; 2.
DR STRING; 192222.Cj1239; -.
DR PaxDb; Q9PN58; -.
DR PRIDE; Q9PN58; -.
DR EnsemblBacteria; CAL35354; CAL35354; Cj1239.
DR GeneID; 905530; -.
DR KEGG; cje:Cj1239; -.
DR PATRIC; fig|192222.6.peg.1221; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_0_7; -.
DR OMA; PINKLAW; -.
DR UniPathway; UPA00244; UER00312.
DR Proteomes; UP000000799; 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 HAMAP; MF_02086; PdxA_Epsilonprot; 1.
DR InterPro; IPR037539; PdxA_epsilonprot.
DR InterPro; IPR005255; PdxA_fam.
DR PANTHER; PTHR30004; PTHR30004; 2.
DR Pfam; PF04166; 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..364
FT /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT /id="PRO_0000188802"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT BINDING 177
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_02086,
FT ECO:0000305|Ref.2"
FT BINDING 216
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_02086,
FT ECO:0000305|Ref.2"
FT BINDING 301
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_02086,
FT ECO:0000305|Ref.2"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3TSN"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:3TSN"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:3TSN"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:3TSN"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:3TSN"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:3TSN"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 103..121
FT /evidence="ECO:0007829|PDB:3TSN"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:3TSN"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:3TSN"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 189..203
FT /evidence="ECO:0007829|PDB:3TSN"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:3TSN"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 226..244
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 248..254
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:3TSN"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 301..311
FT /evidence="ECO:0007829|PDB:3TSN"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:3TSN"
FT STRAND 317..325
FT /evidence="ECO:0007829|PDB:3TSN"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:3TSN"
FT HELIX 348..359
FT /evidence="ECO:0007829|PDB:3TSN"
SQ SEQUENCE 364 AA; 41387 MW; DDD26465821FFC3E CRC64;
MKKLAISIGD INSIGLEILV RSHEELSKIC TPFYFIHESL LNKALKLLNL KLFNAKIVAF
KDDKDYEFNF IKKENSLEIY SFCLPLGFKV DENFEIQAGE IDAKSGLYGF LSFKAASYFV
YEKHAHALLT LPIHKKAWED AGLKYKGHTD ALRDFFKKNA IMMLGCKELF VGLFSEHIPL
AKVSKKITFK NLSIFLKDFY KETHFKKMGL LGFNPHAGDY GVIGGEEEKI MEKAIAFVNA
FLHSKKDEKF FKKALKDENL QKELLLNFKG KGVYLPYPLV ADTAFTKTGL KNCNRLVAMY
HDLALAPLKA LYFDKSINVS LNLPIIRVSV DHGTAFDKAY KNAKINTKSY FEAAKFAINL
HSKA
