ID PDXA_NOSS1 Reviewed; 362 AA. AC P58711; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2002, sequence version 1. DT 27-MAR-2024, entry version 111. DE RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536}; DE EC=1.1.1.262 {ECO:0000255|HAMAP-Rule:MF_00536}; DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536}; GN Name=pdxA {ECO:0000255|HAMAP-Rule:MF_00536}; GN OrderedLocusNames=alr4755; OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576). OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=103690; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576; RX PubMed=11759840; DOI=10.1093/dnares/8.5.205; RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M., RA Takazawa M., Yamada M., Yasuda M., Tabata S.; RT "Complete genomic sequence of the filamentous nitrogen-fixing RT cyanobacterium Anabaena sp. strain PCC 7120."; RL DNA Res. 8:205-213(2001). 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_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:0000255|HAMAP- CC Rule:MF_00536}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00536}; CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00536}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00536}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00536}. CC -!- MISCELLANEOUS: The active site is located at the dimer interface. CC {ECO:0000255|HAMAP-Rule:MF_00536}. CC -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000255|HAMAP- CC Rule:MF_00536}. 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; BA000019; BAB76454.1; -; Genomic_DNA. DR PIR; AC2400; AC2400. DR RefSeq; WP_010998886.1; NZ_RSCN01000020.1. DR AlphaFoldDB; P58711; -. DR SMR; P58711; -. DR STRING; 103690.gene:10496808; -. DR KEGG; ana:alr4755; -. DR eggNOG; COG1995; Bacteria. DR OrthoDB; 9801783at2; -. DR UniPathway; UPA00244; UER00312. DR Proteomes; UP000002483; 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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. 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; Metal-binding; NAD; NADP; Oxidoreductase; KW Pyridoxine biosynthesis; Reference proteome. FT CHAIN 1..362 FT /note="4-hydroxythreonine-4-phosphate dehydrogenase" FT /id="PRO_0000188795" FT BINDING 149 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 184 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_00536" FT BINDING 229 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_00536" FT BINDING 295 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_00536" FT BINDING 303 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 312 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" FT BINDING 321 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536" SQ SEQUENCE 362 AA; 39499 MW; 111DC59550FCCD3E CRC64; MYQLNQNQTV NTPQKYRPRL ALTVGDPGGI GAEVILKALA DLEIGHNYDL TVVSNKNLLQ ETYKQLSSME NLLPLADPNL LKIIDVTVDR ETARQINLGT GNAASGAASF AYMDYAIAQT LAGNFDGIVT GPIAKSAWKA AGYNYPGQTE LLAQKSGVER FGMLFVARSP YTGWTLRALL ATTHIPLRQV ADTLTPQLLT QKLDLLVECL EKDFGITSGR IAIAGLNPHS GEQGQLGTEE LDWLIPWLES ERQKRPHFQL DGPIPPDTMW VKPGQAWYGN AIVQHPADAY LALYHDQGLI PVKLMAFDRA VNTSIGLPFV RTSPDHGTAF DIAGQGIADA TSMKEAISLA AELVCQRLHL EK //