ID   A0A2M7SFQ4_9DELT        Unreviewed;       345 AA.
AC   A0A2M7SFQ4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   13-SEP-2023, entry version 17.
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   ECO:0000313|EMBL:PIZ18367.1};
GN   ORFNames=COY50_15705 {ECO:0000313|EMBL:PIZ18367.1};
OS   Deltaproteobacteria bacterium CG_4_10_14_0_8_um_filter_43_12.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=1973958 {ECO:0000313|EMBL:PIZ18367.1, ECO:0000313|Proteomes:UP000231291};
RN   [1] {ECO:0000313|EMBL:PIZ18367.1, ECO:0000313|Proteomes:UP000231291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG_4_10_14_0_8_um_filter_43_12 {ECO:0000313|EMBL:PIZ18367.1};
RA   Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA   Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA   Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT   "Depth-based differentiation of microbial function through sediment-hosted
RT   aquifers and enrichment of novel symbionts in the deep terrestrial
RT   subsurface.";
RL   Submitted (SEP-2017) 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=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
CC       Note=Binds 1 divalent metal cation per subunit. {ECO:0000256|HAMAP-
CC       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:PIZ18367.1}.
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; PFMT01000457; PIZ18367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M7SFQ4; -.
DR   EnsemblBacteria; PIZ18367; PIZ18367; COY50_15705.
DR   UniPathway; UPA00244; UER00312.
DR   Proteomes; UP000231291; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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}.
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
FT   BINDING         169
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         214
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         269
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         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"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00536"
SQ   SEQUENCE   345 AA;  37054 MW;  9F4FD063EB3CDBCE CRC64;
     MELPVIGITM GDPAGVGPEI IVKALSDPQI FKICRPLVLG DQGIIAKAAQ ILGLEIKVNV
     AKDIRSGRYE VGAINVLNLS NLDASAVAWG KPDERFGKAV VGYIKAGTKL ALEGETEAIT
     TAPINKEVIN RAGYAYAGHT ELFAELTHTK DYVMMLTGEK LRVALVTTHC RLKDVAALLN
     TQRIFTIIKV TNNSLKEYFA ISKPRIAVAS LNPHAGEGGM FGDEEDRIIA PAINRAKDAG
     IHAIGPLPSD TLFYYASRGD YDVVVCMYHD QGLIPLKLLS FQNAVNVTLG LPIIRTSVDH
     GTAYDIAGTG KANPESLKKA ITLAASMANK RRKLSKDMSG NLTLC
//