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Database: UniProt
Entry: A0A0D6MJL6_9PROT
LinkDB: A0A0D6MJL6_9PROT
Original site: A0A0D6MJL6_9PROT 
ID   A0A0D6MJL6_9PROT        Unreviewed;       329 AA.
AC   A0A0D6MJL6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536};
DE            EC=1.1.1.262 {ECO:0000256|HAMAP-Rule:MF_00536};
DE   AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536};
GN   Name=pdxA {ECO:0000256|HAMAP-Rule:MF_00536};
GN   ORFNames=Tasa_010_015 {ECO:0000313|EMBL:GAN53468.1};
OS   Tanticharoenia sakaeratensis NBRC 103193.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Tanticharoenia.
OX   NCBI_TaxID=1231623 {ECO:0000313|EMBL:GAN53468.1, ECO:0000313|Proteomes:UP000032679};
RN   [1] {ECO:0000313|EMBL:GAN53468.1, ECO:0000313|Proteomes:UP000032679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103193 {ECO:0000313|EMBL:GAN53468.1,
RC   ECO:0000313|Proteomes:UP000032679};
RA   Azuma Y., Hadano H., Hirakawa H., Matsushita K.;
RT   "Genome sequencing of Tanticharoenia sakaeratensis NBRC 103193.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00536};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
CC       Note=Binds 1 divalent metal cation per subunit. Can use ions such as
CC       Zn(2+), Mg(2+) or Co(2+). {ECO:0000256|HAMAP-Rule:MF_00536};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
CC       {ECO:0000256|HAMAP-Rule:MF_00536}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00536}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536}.
CC   -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC       {ECO:0000256|HAMAP-Rule:MF_00536}.
CC   -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00536}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAN53468.1}.
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DR   EMBL; BALE01000010; GAN53468.1; -; Genomic_DNA.
DR   RefSeq; WP_048847493.1; NZ_BAQF01000003.1.
DR   AlphaFoldDB; A0A0D6MJL6; -.
DR   STRING; 1231623.Tasa_010_015; -.
DR   OrthoDB; 9801783at2; -.
DR   UniPathway; UPA00244; UER00312.
DR   Proteomes; UP000032679; Unassembled WGS sequence.
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   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   HAMAP; MF_00536; PdxA; 1.
DR   InterPro; IPR037510; PdxA.
DR   InterPro; IPR005255; PdxA_fam.
DR   NCBIfam; TIGR00557; pdxA; 1.
DR   PANTHER; PTHR30004; 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR30004:SF6; D-THREONATE 4-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF04166; PdxA; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00536};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00536}; NAD {ECO:0000256|HAMAP-Rule:MF_00536};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00536}; Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032679};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00536}.
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         161
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         205
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         260
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
SQ   SEQUENCE   329 AA;  34071 MW;  F6CC61A31D9BB21E CRC64;
     MTIPPLALTM GDPAGVGPEL AARAWHALRD TGQPFVWIGD PLLLDGHAPY GIVHEPGHAD
     AVFASALPVL PLTLPAPVTP GTPDPANGAA VVESIARAVE LTLLGRTGAV VTAPIAKSVL
     RAGGFQHPGH TEYLADLCGV AGQEWMMLAS PQLRVVPVTI HVSLRDAIAA LSTDLIVRAG
     RALARALHED LGASGRIAVA GLNPHAGEEG LMGVEDQTIV APAIAILRAE GIAAFGPLPP
     DTMFTEAARR RYDAALCMYH DQALIPLKTL DMAHGVNVTL GLPIVRTSPD HGTAFDIAGT
     GRADPSSLIA ALHMARDMAA TRAAQGHIK
//
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