PDXA_SULDN
ID PDXA_SULDN Reviewed; 307 AA.
AC Q30S58;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Suden_0895;
OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS denitrificans (strain ATCC 33889 / DSM 1251)).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Thiovulaceae; Sulfurimonas.
OX NCBI_TaxID=326298;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33889 / DSM 1251;
RX PubMed=18065616; DOI=10.1128/aem.01844-07;
RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT denitrificans.";
RL Appl. Environ. Microbiol. 74:1145-1156(2008).
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}.
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DR EMBL; CP000153; ABB44173.1; -; Genomic_DNA.
DR RefSeq; WP_011372525.1; NC_007575.1.
DR AlphaFoldDB; Q30S58; -.
DR STRING; 326298.Suden_0895; -.
DR EnsemblBacteria; ABB44173; ABB44173; Suden_0895.
DR KEGG; tdn:Suden_0895; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_0_7; -.
DR OMA; PINKLAW; -.
DR OrthoDB; 1414545at2; -.
DR UniPathway; UPA00244; UER00312.
DR Proteomes; UP000002714; 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; 1.
DR Pfam; PF04166; PdxA; 1.
DR TIGRFAMs; TIGR00557; 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..307
FT /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT /id="PRO_1000051524"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT BINDING 150
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 BINDING 189
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 BINDING 245
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 BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02086"
SQ SEQUENCE 307 AA; 34239 MW; F4ED3F3E89C396FF CRC64;
MSKVRIAISV GDLNGVGIEI AIKAHEEVSK LCAPLYCINS YMLNQASTLL NYKIPSNFEI
SEVGGEFAVK KGCVDKDSGR YSYDSFIHAI SLCEQKKADA VVTMPIHKEA WMLAGLKYKG
HTDLLREHFK RDAIMMLGCQ KMFVALFSEH IPLKDVASSI KYKKLKQFFL DFNNSVPNER
VAVLGLNPHA GDNGVLGNEE LIITKAIKSA NKKVCFEQFI GPLVPDIAFT PHIREKFKYF
IAMYHDQGLA PLKALYFDES INVSLNLPII RTSVDHGTAF DIAYEKKAKT LSYINAIKSA
IALGERL
