ID   A0A2M7SFQ4_9DELT        Unreviewed;       345 AA.
AC   A0A2M7SFQ4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   10-APR-2019, entry version 8.
DE   RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00956571};
DE            EC=1.1.1.262 {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00956565};
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; Proteobacteria; 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.,
RA   Stieglmeier M., Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT   "Depth-based differentiation of microbial function through sediment-
RT   hosted aquifers and enrichment of novel symbionts in the deep
RT   terrestrial subsurface.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-
CC       (phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-
CC       (phosphooxy)butyric acid which spontaneously decarboxylates to
CC       form 3-amino-2-oxopropyl phosphate (AHAP). {ECO:0000256|HAMAP-
CC       Rule:MF_00536, ECO:0000256|SAAS:SAAS01062167}.
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, ECO:0000256|SAAS:SAAS01115138};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00536};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00536};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00536};
CC       Note=Binds 1 divalent metal cation per subunit. Can use ions such
CC       as Zn(2+), Mg(2+) or Co(2+). {ECO:0000256|HAMAP-Rule:MF_00536};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00536,
CC       ECO:0000256|SAAS:SAAS00956575}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00536,
CC       ECO:0000256|SAAS:SAAS00956582}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536,
CC       ECO:0000256|SAAS:SAAS00956573}.
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, ECO:0000256|SAAS:SAAS00701249}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {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   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   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   3: Inferred from homology;
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Complete proteome {ECO:0000313|Proteomes:UP000231291};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536,
KW   ECO:0000256|SAAS:SAAS00956585};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00536};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00536,
KW   ECO:0000256|SAAS:SAAS00701256};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00701266};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00956572};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00536,
KW   ECO:0000256|SAAS:SAAS00701261};
KW   Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00536,
KW   ECO:0000256|SAAS:SAAS00956552};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00536}.
FT   METAL       169    169       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   METAL       214    214       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   METAL       269    269       Divalent metal cation; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     139    139       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     140    140       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     277    277       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     286    286       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00536}.
FT   BINDING     295    295       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                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
//